Title of Invention: COMPOUNDS FOR CONTROL OF APPETITE Abstract: This invention relates generally to neuropeptide Y (“NPY”) Y4 receptor agonists including pancreatic polypeptide (PP), analogs thereof, and peptide fragments of PP, e.g. PP(32-36), and analogs thereof to pharmaceutical compositions containing such Y4 receptor agonists, and to methods for treatment of mammals using the same. The NPY Y4 receptor agonists may be administered to mammals either alone or in combination with NPY Y2 receptor agonists including peptide (PYY) (3-36), analogs thereof and to peptide fragments of PYY(3-36), e.g. PYY(22-36) and PYY(25-36), and analogs thereof such as to control food intake in mammals, blood pressure, cardiovascular response, libido, circadian rhythm, hyperlipidimia, chronic pancreatitis, and nonalcoholic fatty liver disease including nonalcoholic steatohepatitis. Detailed Description: CROSS-REFERENCE TO RELATED APPLICATIONS This application is a divisional of pending U.S. patent application Ser. No. 11/333,889, filed Jan. 18, 2006 (pending), the disclosure of which is hereby incorporated by reference herein. STATEMENT REGARDING FEDERALLY SPONSORED RESEARCH The U.S. Government has a paid-up license in this invention and the right in limited circumstances to require the patent owner to license others on reasonable terms as provided for by the terms of Grant/Contract No. GM47122-08S1 awarded by the National Institutes of Health. FIELD OF THE INVENTION This invention relates generally to neuropeptide Y (“NPY”) Y4 receptor agonists including pancreatic polypeptide (PP), analogs thereof and to peptide fragments of PP, and analogs thereof, and to methods for treatment of mammals using the same and, more specifically, the invention is directed to NPY Y4 receptor agonists including PP(32-36), and analogs thereof, to pharmaceutical compositions containing such pentapeptides, and to methods of treatment of mammals using such pentapeptides. The NPY Y4 receptor agonists may be administered to mammals either alone or in combination with NPY Y2 receptor agonists including peptide YY (PYY) (3-36), analogs thereof, and to peptide fragments of PYY(3-36), and analogs thereof, such as to control food intake in mammals. BACKGROUND OF THE INVENTION Obesity is a major disorder affecting as much as one third of the North American population. Several studies have shown that such individuals are at increased risk in developing cardiovascular disease (hypertension and hyper-cholesterolemia), diabetes and several types of cancer. The effective treatment of obesity, however, remains a largely unachieved goal. Existing pharmaco-therapeutic approaches to weight loss involve the use of amphetamine-based agents such as amphetamine, diethylpropion, mazindol and fenfluramine which act directly on the central nervous system (“CNS”) to lower food intake by modulating dopaminergic, adrenergic and/or serotonergic mechanisms. Although weight loss can be achieved with such agents, their use is restricted due to CNS side-effects, potential addiction liability and the production of tolerance to their actions, with chronic administration leading to potential depression, vestibular disturbances, hallucinations and addiction, as well as interference with the actions of other drugs, such as MAO inhibitors and antihypertensives. There is also a subpopulation of obese patients that is refractory to present anorectic drug treatments. The medical need is high for an effective anorectic agent that overcomes the above disadvantages of existing therapies. Of particular need are agents which act by alternative mechanisms to modulate food intake and/or metabolism. Throughout this application, various publications are referenced. The disclosure of these publications is hereby incorporated by reference into this application to describe more fully the art to which this invention pertains. Neuropeptide Y (“NPY”) Neuropeptides are small peptides originating from large precursor proteins synthesized by peptidergic neurons and endocrine/paracrine cells. They hold promise for treatment of neurological, psychiatric, and endocrine disorders (De Wied, D. In: Neuropeptides: Basics and Perspectives (Elsevier, Amsterdam-New York-Oxford), 1990). Often the precursors contain multiple biologically active peptides. There is great diversity of neuropeptides in the brain caused by alternative splicing of primary gene transcripts and differential precursor processing. The neuropeptide receptors serve to discriminate between ligands and to activate the appropriate signals. Thus, it is expected that the receptors for neuropeptides consist of a large number of members. Neuropeptide Y (NPY), a 36-amino acid peptide, is the most abundant neuropeptide to be identified in mammalian brain. Human NPY has the formula: H-Tyr-Pro-Ser-Lys-Pro-Asp-Asn-Pro-Gly-Glu-Asp-Ala-Pro-Ala-Gfu-Asp-Met-Ala-Arg-Tyr-Tyr-Ser-Ala-Leu-Arg-His-Tyr-Ile-Asn-Leu-Ile-Thr-Arg-Gln-Arg-Tyr-NH2 (SEQ. ID. NO. 1). Porcine and rat NPY have the same sequence except for Leu instead of Met in the 17-position. NPY is an important regulator in both the central and peripheral nervous systems (Heilig, M. and E. Widerlov. Neuropeptide Y: an overview of central distribution, functional aspects, and possible involvement of neuropsychiatric illnesses. Acta Psychiatr. Scand. 82:95-114 (1990)) and influences a diverse range of physiological parameters, including effects on psychomotor activity, food intake, central endocrine secretion, and vasoactivity in the cardiovascular system. High concentrations of NPY are found in the sympathetic nerves supplying the coronary, cerebral, and renal vasculature and has contributed to vasoconstriction. NPY binding sites have been identified in a variety of tissues, including spleen (Lundberg, J. M., A. Hemsen, O. Larsson, A. Rudehill, A. Saria, and B. Fredholm. Neuropeptide Y receptor in pig spleen: binding characteristics, reduction of cyclic AMP formation and calcium antagonist inhibition of vasoconstriction. Bur. J. Pharmacol. 145:21-29 (1988)), intestinal membranes, brain (Hinson, J., C. Rauh, and J. Coupet. Neuropeptide Y stimulates inositol phospholipid hydrolysis in rat brain microprisms. Brain Response. 446:379-382 (1988)), aortic smooth muscle (Mihara, S. Y. Shigeri, and M. Fujimoto. Neuropeptide Y-induced intracellular Ca2+ increase in vascular smooth muscle cells. FEBS Lett. 259: 79-82 (1989)), kidney, testis, and placenta (Dumont, Y., J. C. Martel, A. Fournier, S. St.-Pierre, and R. Quiron. Neuropeptide Y and neuropeptide Y receptor subtypes in brain and peripheral tissues. Prog. Neurobiol. 38:125-167 (1992)). In addition, binding sites have been reported in a number of rat and human cell lines (e.g. Y1 in SK-N-MC, MC-IXC, CHP-212, and PC12 cells; Y2 in SK-N-Be(2), CHP-234, and SMS-MSN)(Grundemar, L., S. P. Sheikh, and C. Wahlestedt; In: The Biology of Neuropeptide Y and Related Peptides. (Humana Press, Inc., Totawa, N.J.), (1992)). NPY forms a family (called the pancreatic polypeptide family) together with pancreatic polypeptide (PP) and peptide YY (PYY) which all consist of 36 amino acids and have a common tertiary structure, the so-called PP-fold (Glover, I. D., D. J. Barlow, J. E. Pitts, S. P. Wood, I. J. Tickle, T. L. Blundell, K. Tatemoto, J. R. Kimmel, A. Wollmer, W. Strassburger, and Y.-S. Zhang. Conformational studies of the pancreatic polypeptide hormone family. Eur. J. Biochem. 142:379-385 (1985)). Specific features of this family include a polyproline helix in residues 1 through 8, beta-turn in residues 9 through 14, an alpha-helix in residues 15 through 30, an outward-projecting C-terminus in residues 30 through 36, and a carboxy terminal amide (Schwartz, T. W., J. Fuhlendorff, L. L. Kjems, M. S. Kristensen, M. Vervelde, M. O'Hare, J. L. Kristenansky, and B. Bjornholm. Signal epitopes in the three-dimensional structure of neuropeptide Y. Ann. N.Y. Acad. Sci. 611:35-47 (1990)). The C-terminal amidated residue of these peptides appears to be essential for biological activity (Wahlestedt et at, 1986). Studies with peptide fragments of NPY have indicated that multiple NPY receptor subtypes exist (Wahlestedt, C., N. Yanaihara, and R. Hakanson, Evidence for different pre- and postjunctional receptors for neuropeptide Y and related peptides. Regal. Pept. 13:307-318 (1986)). Specifically, six receptor subtypes, denoted as Y1 Y2, Y3, Y4, Y5, and Y6, are understood to mediate the actions of NPY with each to-date, except for Y3, having been cloned. The Y1, Y2, Y4, and Y5 receptors have been proposed to regulate feeding behavior, i.e. food intake, in subjects. A key pharmacological feature which distinguishes Y1 from Y2 is the fact that the Y1 receptor (and not the Y2 receptor) responds to an analog of NPY modified at residues 31 and 34 ([Let31,Pro34]NPY), whereas the Y2 receptor (and not the Y1 receptor) has high affinity for the NPY peptide carboxyl-terminal fragment NPY-(18-36)(Fuhlendorff, J., U. Cether, L. Aakerlund, N. Langeland-Johansen, H. Thogersen, S. G. Melberg, U. B. Olsen, O. Thastrup, and T. W. Schwartz. [Leu31,Pro34]Neuropeptide Y: A specific Y1 receptor agonist. Proc. Natl. Acad. Sci. USA 87:182-186 (1990)). NPY analogs and N-terminally-shortened fragments, e.g. NPY(18-36), which contain one or more specific D-isomer substitutions for the naturally occurring residues (as well as pharmaceutically acceptable salts thereof), dispersed in a pharmaceutically acceptable liquid or solid carrier, can be administered to mammals, including humans, to substantially lower blood pressure over an extended period of time or to counteract hypertension. Experimental and clinical observations also have supported the concept that neuropeptides play central roles in neurotransmission as well as the regulation of secretory functions of adenohypophysial, pancreatic, adrenalcortical and gut cells. Among the thirty or so neuropeptides that have been implicated in neuronal function in the mammalian central nervous system, several have also been suggested to function as neurotransmitters or neuromodulators primarily in afferent neurons. An additional action of NPY is to decrease cardiac contractility (inotropy). This is an extremely important action of NPY, because it is known that, under many circumstances in which inotropy is decreased, diseases of life-threatening importance, e.g. congestive heart failure and cardiogenic shock, are associated with probable increased release of NPY into the blood. Prevention of NPY release, using a presynaptic NPY agonist, or NPY's action, using a postsynaptic NPY antagonist, may be beneficial in these disease states. NPY has also been reported to produce coronary artery vasoconstriction and thereby may decrease myocardial blood flow resulting in myocardial ischemia. Such a circumstance can result in angina pectoris or, under more severe circumstances, may result in myocardial infarction and death. In recent years, several classes of drugs have proven effective in dilating coronary arteries to prevent such events. Peptide YY (“PYY”) Peptide YY (PYY) is a 36-residue peptide amide isolated originally from porcine intestine, and localized in the endocrine cells of the gastrointestinal tract and pancreas (Tatemoto et al. Proc. Natl. Acad. Sci. 79:2514, 1982). Peptide YY has N-terminal and C-terminal tyrosine amides; accordingly, these two tyrosines give PYY its name (Y represents the amino acid tyrosine in peptide nomenclature). In addition, PYY shares a number of central and peripheral regulatory roles with its homologous peptide Neuropeptide Y (NPY), which was originally isolated from porcine brain (Tatemoto, Proc. Natl. Acad. Sci. 79:5485, 1982). PYY is localized in intestinal cells; NPY, in contrast, is present in the submucous and myenteric neurons that innervate the mucosal and smooth muscle layers, respectively (Ekblad et al. Neuroscience 20:169, 1987). Both PYY and NPY are believed to inhibit gut motility and blood flow (Laburthe, Trends Endocrinol. Metab. 1: 168, 1990), and they are also thought to attenuate basal (Cox et al. Br. J. Pharmacol. 101:247, 1990; Cox et al. J. Physiol. 398:65, 1988; Cox et al. Peptides 12:323, 1991; Friel et al. Br. J. Pharmacol. 88:425, 1986) and secretatogue-induced intestinal secretion in rats (Lundberg et al. Proc. Natl. Acad. Sci USA 79:4471, 1982; Playford et al. Lancet 335: 1555, 1990) and humans (Playford et al., supra), as well as stimulate net absorption (MacFadyen et al. Neuropeptides 7:219, 1986). Elevated plasma PYY levels have been reported in individuals suffering from several conditions that cause diarrhea (Adrian et al. Gastroenterology 89:1070, 1985). Taken together, these observations suggest that PYY and NPY are released into the circulation after a meal (Adrian et al. Gastroenterology 89:1070, 1985: Balasubramaniam et al. Neuropeptides 14:209, 1989), and, thus may play a physiological role in regulating intestinal secretion and absorption, serving as natural inhibitors of diarrhea. A high affinity PYY receptor system that exhibits a slightly higher affinity for PYY than NPY has been characterized in rat intestinal epithelia (Laburthe et al. Endocrinology 118:1910, 1986; Laburthe, Trends Endocrinol. Metabl. supra) and shown to be negatively coupled to adenylate cyclase (Servin et al. Endocrinology 124:692, 1989). Consistently, PYY exhibited greater antisecretory potency than NPY in voltage clamped preparations of rat small intestine (Cox et al. J. Physiol supra), while C-terminal fragments of NPY were found to be less effective in their antisecretory potency than PYY (Cox et al. Br. J. Pharmacol, supra), Structure-activity studies using several partial sequences have led to the identification of PYY(22-36) as the active site for interacting with intestinal PYY receptors (Balasumbramaniam et al. Pept. Res. 1:32, 1988). This intestinal PYY-preferring receptor has now been cloned and shown to be identical to the Y2 receptors cloned from the brain (Goumain et al. Mol Pharmacol 60:124-134, 2001). In addition, PYY has been implicated in a number of physiological activities including nutrient uptake (see, e.g., Bilcheik et al. Digestive Disease Week 506:623, 1993), cell proliferation (see, e.g., Laburthe, Trends Endocrinol. Metab. 1:168, 1990; Voisin et al. J. Bio. Chem., 1993), lipolysis (see, e.g., Valet et al. J. Clin. Invest. 85:291, 1990), and vasoconstriction (see, e.g., Lundberg et al., Proc. Natl. Acad. Sci, USA 79:4471, 1982). The amino acid sequences of porcine and human PYY are as follows: (SEQ. ID. NO. 2) porcine PPY: YPAKPEAPGEDASPEELSRYYASLRHYLNLVTRQRY, (SEQ. ID. NO. 3) human PYY: YPIKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY. The amino acid sequences for dog PYY and for rat PYY are the same as that of porcine PYY. With respect to PYY, it has been reported previously that peripheral administration of PYY(3-36), a NPY Y2-preferring ligand, can on peripheral administration attenuate food intake in normal and fasted mice and rats as well as in normal and obese humans (Nature 418:650-654; 2002, N Engl J Med 349:941-948; 2003). The anorexigenic actions of PYY(3-36) are suggested to be mediated by arcuate nucleus Y2 receptors. one advantage of using Y2 selective ligands is that they can suppress the food intake on peripheral administration, whereas Y1 and Y5 selective ligands, as described above, have to penetrate the BBB to modulate food intake. In addition to interacting with the Y2 receptor, PYY(3-36) can potently activate Y4 and Y5 receptors. Consequently, the inventor previously developed Y2 receptor selective agonists that are based on PYY(22-36) and PYY(25-36) (See U.S. Pat. Nos. 5,604,203, and 6,046,167 to Balasubramaniam) which are devoid of activities at the other NPY receptors including Y1, Y4, and Y5 at concentrations up to 20,000 nM. Preferred PYY(25-36) analogs include N-α-Ac-[Trp30]PYY(25-36)-NH2 (SEQ. ID. NO. 4), referred to as BWX-115, N-α-Ac-[Trp27, Ψ35/36]PY(25-36)-NH2 (SEQ. ID. NO. 5), referred to as BT-56, and N-α-Ac-[Trp30, Ψ35/36]PYY(25-36)-NH2 (SEQ. ID. NO. 6), referred to as BT-123, and the PYY(22-36) analog N-α-Ac[Nle24,28, Tr30, Nva31, Ψ35/36]PY(22-36)-NH2 (SEQ. ID. NO. 7), referred to as B-48, [wherein ψ in the foregoing formulas is —CH2-NH—] which can be used to control food intake in animals and humans. Pancreatic Peptide (“PP”) Pancreatic peptide (PP) is a 36-amino-acid secretory peptide that is predominantly produced by the pancreas and released in response to nutrient stimuli. The amino acid sequence of human PP is as follows: (SEQ. ID. NO. 8) APLEPVYPGDNATPEQMAQYAADLRRYINMLTRPRY. PP, like PYY, shares a number of central and peripheral regulatory roles with its homologous peptide NPY. It has been reported recently that PP can attenuate body weight increase in mice through inhibiting food intake and increasing energy expenditures (Gastroenterology 124:1325-1336; 2003). These actions are mediated by altering the expression of orexigenic (NPY, orexin & ghrelin downregulated) and anorexigenic (urocortin upregulated) peptides, and decreasing gastric emptying and activity of the vagovagal or vago-sympathetic reflex arc. In addition, the anorectic effects of PP have been suggested to be mediated by the Y4 receptors in the area postrema (AP) because: a) autoradiography following peripheral administration of PP revealed high accumulation of PP in AP; b) expression of c-fos is seen in AP following iv administration of PP; and c) high density of Y4 receptors are present in AP (Brain Res 760:137-149; 1997). one advantage of using Y4 selective ligands, like the Y2 selective ligand, is that they can suppress the food intake on peripheral administration, whereas Y1 and Y5 selective ligands, as described above, have to penetrate the BBB to modulate food intake. Native PP may not be an ideal candidate for suppressing food intake because of its short half-life of about six minutes and its interactions with Y5 receptors. Accordingly, it would be desirable to develop NPY Y4 receptor agonists that can be used alone or mixed with NPY Y2 receptor agonists, as disclosed in U.S. Pat. Nos. 5,604,203, and 6,046,167 to Balasubramaniam, which are herein incorporated by reference, for controlling an NPY mediated physiological response in a subject, such as to control food intake in mammals, and that are expected to prove useful in the treatment of weight problems (e.g. obesity and diabetes), eating disorders, and such. SUMMARY OF THE INVENTION This invention is directed to neuropeptide Y (“NPY”) Y4 receptor agonists including pancreatic polypeptide (PP), analogs thereof, and peptide fragments of PP, e.g. PP(32-36), and analogs thereof, to pharmaceutical compositions containing such Y4 receptor agonists, and to methods for treatment of mammals using the same. The NPY Y4 receptor agonists may be administered to mammals either alone or in combination with NPY Y2 receptor agonists including peptide YY (PYY) (3-36)5 analogs thereof, and to peptide fragments of PYY(3-36), e.g. PYY(22-36) and PYY(25-36), and analogs thereof, as disclosed in U.S. Pat. Nos. 5,604,203, and 6,046,167 to Balasubramaniam, which are herein incorporated by reference, such as to control food intake in mammals, blood pressure, cardiovascular response, libido, circadian rhythm, hyperlipidimia, chronic pancreatitis, and nonalcoholic fatty liver disease including nonalcoholic steatohepatitis. Accordingly, in one aspect, the present invention features NPY Y4 receptor agonists of PP(32-36) and analogs thereof, such pentapeptide analogs having the formula: wherein: each X, independently, is an aromatic amino acid; each Y, independently, is an amino acid having a guanidino group; each Z, independently, is an aliphatic amino acid; n=1, 2, 3 or 4; and wherein the compound optionally includes one or two pseudopeplide bonds where each pseudopeptide bond is independently selected from —CH2NH—, —CH2—S—, —CH2CH2—, —CH2—O— and CH2—CO—. A preferred compound of formula (I) includes, (which is referred to as B-74). In another aspect, the present invention features pentapeptide analogs of PP(32-36) having the formula: wherein. each X, independently, is an aromatic amino acid; each Y, independently, is an amino acid having a guanidino group; each Z, independently, is an aliphatic amino acid; A1 and A2, independently, are selected ftom Cys, Pen, Glu, Asp, Lys, and Dpr; and wherein the compound optionally includes one or two pseudopeptide bonds where each pseudopeptide bond is independently selected from —CH2—NH—, —CH2S—, —CH2—C2—, —CH2—O— and CH2—CO—. A preferred compound of formula (II) includes, In another aspect, the present invention features pentapeptide analogs of PP(32-36) having the formula: H—[X—Y-Z-Y—X]n—NH2 (III) wherein: each X, independently, is an aromatic amino acid; each Y, independently, is an amino acid having a guanidino group; each Z, independently, is an aliphatic amino acid; n=1, 2, 3 or 4; and wherein the compound optionally includes one or two pseudopeptide bonds where each pseudopeptide bond is independently selected from —CH2—NH—, —CH2—S—, —CH2—CH2—, —CH2—O— and CH7—CO—. Preferred compounds of formula (III) include H-Tyr-Arg-Leu-Arg-Tyr-Tyr-Arg-Leu-Arg-Tyr-NH2 (SEQ. ID. NO. 9) or H-Tyr-Arg-Leu-Arg-Tyr-Tyr-Arg-Leu-Arg-Tyr-Tyr-Arg-Leu-ArgTyr-NH2 (SEQ. ID. NO. 10). In another aspect, NPY Y4 receptor agonists, such as those of formulas (I-III), are mixed or combined with NPY Y2 receptor agonists, such as analogs of PYY(25-36) or PYY(22-36), for controlling an NPY mediated physiological response in a subject, e.g. to suppress appetite, such analogs of PYY(25-36) and of P(22-36), respectively, having formulas (IV) and (V) below: wherein: the N-terminal amino acid is bonded to R1 and R2; Y is a chain of 0-4 amino acids, inclusive, where the C-terminal amino acid has a carboxylamide group; which is independently bonded to R3 and R4, e.g., R1 and R2 are each independently bonded to the amino group of the N-terminal amino acid and selected from H, (C1-C12)alkyl, (C6-C18)acyl, (C1-C12)acyl, (C7-C18) aralkyl, and (C7-C18)alkaryl; R3 and R4 are each independently bonded to the amide group of the C-terminus amino acid, e.g., (where R denotes the side chain group of the amino acid, e.g. R═H in Gly, etc.), and selected from H, (C1-C12)alkyl (e.g. methyl), (C6-C18)aryl (e.g. phenyl), (C1-C12)acyl (formyl, acetyl, napthateneacetyl, and myristoyl), (C7-C18) aralkyl (e.g. benzyl), and (C7-C18)alkaryl (e.g. p-methlyphenyl); A25 is Arg, Lys, homo-Arg, diethyl-homo-Arg, lys-ε-NH—R where R is H, a branched or straight chain (C1-C10) alkyl group, or an aryl group, Orn or is deleted; A26 is Ala, His, Thr, 3-Me-His, 1-Me-His, β-pyrozolyiaianin, N-Me-His, Arg, Lys, homo-Arg, diethyl-homo-Arg, Lys-e-NH—R where R is H, a branched or straight chain (C1-C10) alkyl group, or an aryl group, Orn or is deleted; A27 is an aromatic amino acid: A28 is Leu, Ile, Val, Tip Nle, Nva, Aib, Anb, or N-Me-Leu; A29 is Asn, Ala, Gln, Fly, Trp, or N-Me-Asn; A30 is Leu, Ile, Val, Trp, Nle, Nva, Aib, Anb, or N-Me-Leu; A31 is Val, Ile, Trp, Nva, Aib, Anb, or N-Me-Val; A32 is Thr, Ser, N-Me-Ser, N-Me-Thr, or D-Trp; and wherein the compound optionally includes one or two pseudopeptide bonds where each pseudopeptide bond is independently selected from —CH2—NH—, —CH2— S—, —CH2—CH2—, —CH2—O— and C2—CO—; wherein X is a chain of 0-5 amino acids, inclusive, where the N-terminal amino acid is bonded to R1 and R2 by the nitrogen of the amino group of the N-terminal amino acid; Y is a chain of 0-4 amino acids, inclusive, where the C-terminal amino acid has a carboxylamide group; which is independently bonded to R3 and R4, e.g., R1 and R2 are each independently bonded to the amino group of the N-terminal amino acid and selected from H, (C1-C12)alkyl, (C6-C18)aryl, (C1-C12)acyl, (C7-C18) aralkyl, and (C7-C18)alkaryl; R3 and R4 are each independently bonded to the amide group of the C-terminus amino acid, e.g., (where R denotes the side chain group of the amino acid, e.g. R═H in Gly, etc.), and selected from H, (C1-C12)alkyl (e.g. methyl), (C6-C18)aryl (e.g. phenyl), (C1-C12)acyl (formyl, acetyl, napthaleneacetyl, and myristoyl), (C7-C18)aralkyl (e.g. benzyl), and (C7-C18)alkaryl (e.g. p-methlyphenyl); A22 is an aromatic amino acid, Ala, Aib, Anb, N-Me-Ala or is deleted; A23 is Ser, Thr, Ala, Aib, N-Me-Ser, N-Me-Thr, N-Me-Ala or is deleted; A24 is Leu, Ile, Nle, Val, Trp, Gly, Nva, Aib, Anb, N-Me-Leu or is deleted; A25 is Arg, Lys, homo-Arg, diethyl-homo-Arg, Lys-pε-NH—R (where R is H, a branched or straight chain (C1-C10) alkyl group, or an aryl group), Orn or is delete; A26 is Ala, His, Thr, 3-Me-His, 1-Me-His, β-pyrazolylalaline, N-Me-His, Arg, Lys, homo-Arg, diethyl-homo-Arg, Lys-F—NH—R (where R is H, a branched or straight chain (C1-C10) alkyl group, an aryl group, or a pharmaceutically acceptable salt thereof), Orn or is deleted; A27 is an aromatic amino acid; A is Leu, Ile, Nle, Val, Trp, Aib, Anb or N-Me-Leu; A29 is Asn, Ala, Gln, Gly, Trp or N-Me-Asn; A30 is Leu, Ile, Nle, Nva, Fla, Val, Trp, Aib, Anb or N-Me-Leu; A31 is Val, Len, Nle, Nva, Ile, Trp, Aib, Anb or N-Me-Val; A32 is Thr; Ser, D-Trp, N-Me-Ser or N-Me-Thr; and wherein the compound optionally includes one or two pseudopeptide bonds where each pseudopeptide bond is independently selected from —CH2—NH—, —CH2—S—, —CH2—CH2—, CH2—O— and CH2—CO—. A preferred compound of formula (IV) includes N-α-Ac[Trp27, ψ35/36]PYY(25-36)-NH2 (SEQ. ID. NO. 5), referred to as BT-56, N-α-Ac[Trp30]PYY(25-36)-NH2 (SEQ. ID. NO. 4), referred to as BWX-15, and N-α-Ac-[Trp30, ψ35/36]PYY(25-36)-NH2 (SEQ. ID. NO. 6), referred to as BT-123, wherein N in the foregoing formulas is —CH2-NH—. A preferred compound of formula (V) includes N-α-Ac[Nle24,28, Trp30 Nva31, ψ35/36]PYY(22-36)-NH2 (SEQ. ID. NO. 7) referred to as B-48, wherein NV is —CH2-NH—. The formulas of I-V, as indicated above, optionally include at least one pseudopeptide bond between amino acid residues, By “psuedopeptide bond” is meant that the carbon atom participating in the bond between two residues is reduced from a carbonyl carbon to a methylene carbon, i.e., CH2—NH; or less preferably that of CO—NH is replaced with any of CH2—S, CH2—CH2, CH2—O, or CH2—CO. A psuedopeptide bond may be symbolized herein by “ψ”. The psuedopeptide bond analogs can be used to form dimeric analogs. A detailed discussion of psuedopeptide bonds is given in Coy et al. (1998) Tetrahedon 44:835-841. In another aspect, the invention features a method of controlling the food intake, i.e. appetite, of a subject comprising administering to said subject the compound of formula I, II, or III alone or in combination with formulas IV or V. In other preferred embodiments, a therapeutically effective amount of a compound of formula I, II, or III alone, or in combination with formulas IV or V, and a pharmaceutically acceptable carrier substance together form a therapeutic composition capable of suppressing an NPY mediated physiological response. BRIEF DESCRIPTION OF THE FIGURES FIG. 1 is a graph representing the feeding patterns of animals treated with a PP(32-36) analog by intraperitoneal injection. The compounds tested include a control (saline), hPP, and FIG. 2 is a graph representing the feeding patterns of animals treated with a PP(32-36) analog (Y4 receptor agonist), and a mixture of the PP(32-36) analog and a PYY(22-36) analog (Y2 receptor agonist), by intraperitoneal injection. The compounds tested include a control (saline), and a combination of B-74 and N-α-Ac[Nle24,28, Trp30, Nva3, ψ35/36]PYY(22-36)-NH2 (SEQ. ID. NO 7) (B-48) wherein ψ is —CH2-NH—; and FIG. 3 is a graph representing the feeding patterns of animals treated with a PYY(22-36) analog (Y2 agonist receptor), and a mixture of the PYY(22-36) analog and a PP(32-36) analog (Y4 receptor agonist), by intraperitoneal injection. The compounds tested include a control (saline), N-α-Ac[Nle24,28, Trp30, Nva31, ψ35/36]PYY(22-36)-NH2 (SEQ. ID. NO. 7) (B-48) wherein ψ is —CH2—NH—, and a combination of B-48 and DETAILED DESCRIPTION OF THE INVENTION The present invention is directed to neuropeptide Y (“NPY”) Y4 receptor agonists including pancreatic polypeptide (PP), analogs thereof, and peptide fragments of PP, e.g. PP(32-36), and analogs thereof, to pharmaceutical compositions containing such Y4 receptor agonists, and to methods for treatment of mammals using the same. The NPY Y4 receptor agonists may be administered to mammals either alone or in combination with NPY Y, receptor agonists including peptide YY (PYY) (3-36), analogs thereof, and to peptide fragments of P (3-36), e.g. PYY(22-36) and PYY(25-36), and analogs thereof, such as to control food intake in mammals, blood pressure, cardiovascular response, libido, circadian rhythm, hyperlipidimia, chronic pancreatitis, and nonalcoholic fatty liver disease including nonalcoholic steatohepatitis. one advantage of using the Y4 selective ligands of the present invention is that they can suppress food intake on peripheral administration, whereas Y1 and Y5 selective ligands, as described above, have to penetrate the BBB to modulate food intake. Additionally, an advantage of using Y2 selective ligands is that they also can suppress the food intake oil peripheral administration. Therefore, the inventor has developed NPY Y4 receptor agonists that can be used alone or mixed with NPY Y2 receptor agonists, as are disclosed in U.S. Pat. Nos. 5,604,203, and 6,046,167 to Balasubramaniam, which are herein incorporated by reference, for controlling an NPY mediated physiological response in a subject, such as to control food intake in mammals by suppressing appetite. Accordingly, in one aspect, the present invention features NPY Y4 receptor agonists of PP(32-36) and analogs thereof, such pentapeptide analogs having the formula: wherein: each X, independently, is an aromatic amino acid; each Y, independently, is an amino acid having a guanidino group; each Z, independently, is an aliphatic amino acid; n=1, 2, 3 or 4; and wherein the compound optionally includes one or two pseudopeptide bonds where each pseudopeptide bond is independently selected from —CH—NH—, —CH2—S—, —CH2—C2—, —CH2—O— and CH2—CO—. A preferred compound of formula (I) includes, (which is referred to as B-74). In another aspect, the present invention features NPY Y4 receptor agonists or pentapeptide analogs of PP(32-36) having the formula: wherein: each X, independently, is an aromatic amino acid; each Y, independently, is an amino acid having a guanidino group; each Z, independently, is an aliphatic amino acid; A1 and A2, independently, are selected from Cys, Pen, Glu, Asp, Lys, and Dpr; and wherein the compound optionally includes one or two pseudopeptide bonds where each pseudopeptide bond is independently selected from —CH2—NH—, —CH2—S—, —CH2—CH2—, —CH2—O— and CH2—CO—. A preferred compound of formula (II) includes, In another aspect, the present invention features NPY Y4 receptor agonists or pentapeptide analogs of PP(32-36) having the formula: H—[X—Y-Z-Y—X]n—NH2 (III) wherein: each X, independently, is an aromatic amino acid; each Y, independently, is an amino acid having a guanidino group; each Z, independently, is an aliphatic amino acid; n=1, 2, 3 or 4; and wherein the compound optionally includes one or two pseudopeptide bonds where each pseudopeptide bond is independently selected from CH2—NH—, —CH2—S—, —CH2—CH2—, —CH2—O— and CH2—CO—. Preferred compounds of formula (II) include H-Tyr-Arg-Leu-Arg-Tyr Tyr-Arg-Leu-Arg-Tyr-NH12 (SEQ. ID. NO. 9) or H-Tyr-Arg-Leu-Arg-Tyr-Tyr-Arg-Leu-Arg-Tyr-Tyr-Arg-Leu-Arg-Tyr-NH2 (SEQ. ID. NO. 10). For formulas I-III, aromatic amino acids can include, for example, phenylalanine, tryptophan, or tyrosine, which is a hydroxyl aromatic amino acid; aliphatic amino acids can include, for example, isoleucine, leucine, norvaline, glycine, alanine, or valine; and amino acids that have a guanidino group may include, for example, arginine. In addition, the C-terminal of the compounds of formulas (I-III) are amidated. In another aspect, NPY Y4 receptor agonists, such as those of formulas (I-III), are mixed or combined with NPY Y2 receptor agonists, such as analogs of PYY(25-36), for controlling an NPY mediated physiological response in a subject, e.g. to suppress appetite, such analogs of PYY(25-36) having the formula: wherein: the N-terminal amino acid is bonded to R1 and R2; Y is a chain of 0-4 amino acids, inclusive, where the C-terminal amino acid has a carboxyl amide group; which is independently bonded to R3 and R4, e.g., R1 and R2 are each independently bonded to the amino group of the N-terminal amino acid and selected from H, (C1-C12)alkyl (e.g. methyl), (C6-C18)aryl (e.g. phenyl), (C1-C12)acyl (formyl, acetyl, napthaleneacetyl, and myristoyl), (C7-C18)aralkyl (e.g. benzyl), and (C7-C18)alkaryl (e.g. p-methlyphenyl); R3 and R4 are each independently bonded to the amide group of the C-terminus amino acid, e.g., (where R denotes the side chain group of the amino acid, e.g. R═H in Gly, etc.), and selected from H, (C1-C12)alkyl (e.g. methyl), (C6-C18)aryl (e.g. phenyl), (C1-C12)acyl (formyl, acetyl, napthaleneacetyl, and myristoyl), (C7-C18)aralkyl (e.g. benzyl), and (C7-C18)alkaryl (e.g. p-methlyphenyl); A25 is Arg, Lys, homo-Arg, diethyl-homo-Arg, lys-ε-NH—R (where R is H, a branched or straight chain (C1-C10) alkyl group, or an aryl group), Orn or is deleted; A26 is Ala, His, Thr, 3-Me-His, 1-Me-His, β-pyrozolylalanin, N-Me-His, Arg, Lys, homo-Arg, diethyl-homo-Arg, Lys-e-NH—R (where R is H, a branched or straight chain (C1-C10) alkyl group, or an aryl group), Orn or is deleted; A27 is an aromatic amino acid: A28 is Leu, Ile, Val, Trp Nle, Nva, Aib, Anb, or N-Me-Leu; A29 is Asn, Ala, Gln, Fly, Trp, or N-Me-Asn; A30 is Leu, Ile, Val, Trp, Nle, Nva, Aib, Anb, or N-Me-Leu; A31 is Val, Ile, Trp, Nva, Aib, Anb, or N-Me-Val; A32 is Thr, Ser N-Me-Ser, N-Me-Thr, or D-Trp. In preferred embodiments Y is A33-A34-A35-A36 wherein A33 is Arg, Lys, homo-Arg, diethyl-homo-Arg, Lys-F—NH—R (where R is H, a branched or straight chain (C1-C10) alkyl group, or (C6-C18) aryl group), Cys, or Orn A34 is Gln, Asn, Ala, Gly, N-Me-Gln, Aib, Cys, or Anb; A35 is Arg, Lys, homo-Arg, diethyl-homo-Arg, Lys-ε-NH—R (where R is H, a branched or straight chain (C1-C10) alkyl group, or (C6-C18) aryl group), Cys, or Orn; and A36 is an aromatic amino acid, Cys, or a pharmaceutically acceptable salt thereof. Most preferably, the compound of formula (IV) includes N-α-Ac[Trp27, ψ35/36]PYY(25-36)-NH2 (SEQ. ID. NO. 5), referred to as BT-56, and N-α-Ac[Trp3]PYY(25-36)-NH2 (SEQ. ID. NO. 4), referred to as BWX-115, and N-α-Ac-[Trp30, ψ35/36]PYY(25-36)-NH2 (SEQ. ID. NO. 6), referred to as BT-1123, wherein y in the foregoing formulas is —CH2—NH—. In yet another aspect, NPY Y4 receptor agonists, such as those of formulas (I-III), are mixed with NPY Y2 receptor agonists, such as analogs of PYY(22-36), for controlling an NPY mediated physiological response in a subject, e.g. to suppress appetite, such analogs of PYY(22-36) having the formula: wherein X is a chain of 0-5 amino acids, inclusive, where the N-terminal amino acid is bonded to R1 and R2 by the nitrogen of the amino group of the N-terminal amino acid; Y is a chain of 0-4 amino acids, inclusive, where the C-terminal amino acid has a carboxylamide group; which is independently bonded to R3 and R4, e.g., R1 and R2 are each independently bonded to the amino group of the N-terminal amino acid and selected from H, (C1-C12)alkyl (e.g. methyl), (C6-C18)aryl (e.g. phenyl), (C1-C12)acyl (formyl, acetyl, napthaleneacetyl, and myristoyl), (C7-C18)aralkyl (e.g. benzyl), and (C7-C18)alkaryl (e.g. p-methlyphenyl); R3 and R4 are each independently bonded to the amide group of the C-terminal amino acid, e.g., (where R denotes the side chain group of the amino acid, e.g. R═H in Gly, etc.), and selected from H, (C1-C12)alkyl (e.g. methyl), (C6-C18)aryl (e.g. phenyl), (C1-C12)acyl (formyl, acetyl, napthaleneacetyl, and myristoyl), (C7-C18)aralkyl (e.g. benzyl), and (C7-C18)alkaryl (e.g. p-methlyphenyl); A22 is an aromatic amino acid, Ala, Aib, Anb, N-Me-Ala or is deleted; A23 is Ser, Thr, Ala, Aib, N-Me-Ser, N-Me-Thr, N-Me-Ala or is deleted; A24 is Leu, Ile, Nle, Val, Trp, Gly, Nva, Aib, Anb, N-Me-Leu or is deleted; A25 is Arg, Lys, homo-Arg, diethyl-homo-Arg, Lys-pε-NH—R (where R is H, a branched or straight chain (C1-C10) alkyl group, or an aryl group), Orn or is deleted; A26 is Ala, His, Thr, 3-Me-His, 1-Me-His, β-pyrazolylalaline, N-Me-His, Arg, Lys, homo-Arg, diethyl-homo-Arg, Lys-ε-NH—R (where R is H, a branched or straight chain (C1-C10) alkyl group, an aryl group, or a pharmaceutically acceptable salt thereof), Orn or is deleted; A27 is an aromatic amino acid; A28 is Leu, Ile, Nle, Val, Trp, Aib, Anb or N-Me-Leu; A29 is Asn, Ala, Gln, Gly, Trp or N-Me-Asn; A30 is Leu, Ile, Nle, Nva, Fla, Val, Trp, Aib, Anb or N-Me-Leu; A31 is Val, Leu, Nle, Nva, Ile, Trp, Aib, Anb or N-Me-Val; and A32 is Thr, Ser, D-Trp, N-Me-Ser or N-Me-Thr. In preferred embodiments, Y is A33-A34-A35-A36 wherein A33 is Arg, Lys, homo-Arg, diethyl-homo-Arg, Lys-ε-N—HR (where R is U, a branched or straight chain (C1-C10) alkyl group, or an aryl group), Cys, or Orn A34 is Cys, Gln, Asn, Ala, Gly, N-Me-Gln, Aib, or Anb; A35 is Arg, Lys, homo-Arg, diethyl-homo-Arg, Lys-ε-NH—R (where R is U, a branched or straight chain (C1-C10) alkyl group, or an aryl group), Cys, or Orn; and A36 is an aromatic amino acid, Cys, or a pharmaceutically acceptable salt thereof. Most preferably, the compound of formula (V) includes N-α-Ac[Nle24,25, Trp30, Nva31, ψ35/36]PYY(22-36)-NH, (SEQ. ID. NO. 7) referred to as B-48, wherein ψ is —CH2NH—. Concerning formulas IV and V, reference to the (C1-C12)acyl for R1 and R2 can include an aliphatic acyl (e.g. CH3CO) or an aromatic acyl (e.g. C6H5CO). Additionally, the formulas of I-V optionally include at least one pseudopeptide bond between amino acids residues. By “psuedopeptide bond” is meant that the carbon atom participating in the bond between two residues is reduced from a carbonyl carbon to a methylene carbon, i.e., CH2-NH; or less preferably that of CO—NH is replaced with any of CH2—S, CH2—CH2, CH2—O, or CH2—CO. A psuedopeptide peptide bond is symbolized herein by “ψ”. Preferably, the psuedopeptide bonds are located between one or more amino acid residues. In addition, such psuedopeptide bond analogs can be used to form dimeric analogs. A detailed discussion of psuedopeptide bonds is given in Coy et al., (1998) Tetrahedon 44:835-841. Accordingly, in another aspect and as already specifically illustrated by certain of the preferred compounds, the invention features dimers, trimers, etc. of compounds having the formula (I-V). These dimers, trimers, etc. may be prepared, for example, by dimerizing compounds of formula (I-V) with dicarboxylic acids (e.g., succinic acid), cystine, or diaminodicarboxylic acid (e.g., 2,6-diaminopimelic acid) as is known in the art. Resulting compounds can include, for example, pentapeptide linear tandem or parallel dimers. In another aspect, the invention features a method of controlling the food intake, i.e. appetite, of a subject comprising administering to said subject the compound of formula I, II, or III alone or in combination with formulas IV or V. These compounds also can be conjugated to carriers, such carriers can include albumin, such as cationized albumin (Endocrinology 126:977-984 (1990); J. Pharmacol Exp. Therao. 268:791-796 (1994)), polyethylene glycol, polyglutamic acid, polyleucine, polyisoleucine or polylysine, e.g., MAP. In other preferred embodiments, a therapeutically effective amount of a compound of formula I, II, or III alone, or in combination with formulas IV or V, and a pharmaceutically acceptable carrier substance, e.g., magnesium carbonate or lactose, together form a therapeutic composition capable of suppressing an NPY mediated physiological response. This composition call be in the form of a pill, tablet, capsule, liquid, or sustained released tablet for oral administration; or a liquid for nasal administration as drops or spray; or a liquid for intravenous, subcutaneous, parenteral, or intraperitoneal administration. Another preferred form for administration includes a biodegradable sustained-release composition for intramuscular administration to a subject in need of the composition. Preferably, the composition includes a lipophilic salt and is suitable for administration in the form of an oil emulsion or dispersion to a subject in need of the composition. In yet another aspect, the invention features methods for controlling an NPY mediated physiological response in a subject; such methods involve administering a compound of formula I, II, or III alone, or in combination with formulas IV or V, to a subject in a dosage effective to control blood pressure, cardiovascular response, libido, circadian rhythm, hyperlipidimia, chronic pancreatitis, and nonalcoholic fatty liver disease including nonalcoholic steatohepatitis. The NPY Y4 receptor agonists including pancreatic polypeptide (PP), analogs thereof, and peptide fragments of PP, e.g. PP(32-36), and analogs thereof such as those of compounds (I-III), either alone or in combination with NPY Y2 receptor agonists including peptide YY (PYY) (3-36), analogs thereof, and to peptide fragments of PYY(3-36), e.g. PYY(22-36) and PYY(25-36), and analogs thereof such as those of compounds (IV-V), also can be useful in treating any number of illnesses that involve eating disorders, cardiovascular function, alterations in sexual function, as well as disorders of sleep and circadian rhythms (see, e.g., Harrison's Principles of Internal Medicine, McGraw-Hill Inc., New York, 12th ed.). Other features and advantages of the invention will be apparent to one skilled in the art. The symbol A1, A2, A3, and the like; and Tyr, Lys or the like, as found in a peptide sequence herein stands for an amino acid residue, e.g., —N—CH(R)—CO— when it is at the N-terminus, or —NH—CH(R) —CO— when it is at any other position, where R denotes the side chain (or identifying group) of an amino acid or its residue. For example, R is CH2COOH for Asp, R is —H for Gly, R is —CH2OH for Ser, R is —CH3 for Ala and R is —CH2CH2CH2CH2NH2 for Lys. As set forth above and for convenience in describing this invention, the conventional and certain unconventional abbreviations for the various amino acids are used. They are familiar to those skilled in the art; but for clarity are listed below, All peptide sequences mentioned herein are written according to the usual convention whereby the N terminal amino acid is on the left and the C-terminal amino acid is on the right. A short line between two amino acid residues indicates a peptide bond. Abbreviations (common): Asp=D Aspartic Acid Ala=A=Alanine Arg=R=Arginine Asn=N=Asparagine Cys=C=Cysteine Gly=G=Glycine Glu=E=Glutamic Acid Gln Q=Glutamine His=H=Histidine Ile=I=Isoleucine Leu=L=Leucine Lys=K=Lysine Met=M=Methionine Phe=F=Phenylalanine Pro=P=Proline Ser=S=Serine Thr=T=Threonine Trp=W=Tryptophan Tyr=Y=Tyrosine Val=V=Valine. Abbreviations (uncommon). Aoc=8-aminooctanoic acid Orn=Ornithine Nal=2-napthylalanine Thi=2-thienylalanine Pcp=4-chlorophenylalanine Bth=3-benzothienyalanine Bip=4,4′-biphenylalanine Tic=tetrahydroisoquinoline-3-carboxylic acid Aib=aminoisobutyric acid Anb=alpha-aminonornalbutyric acid Ac6c=1-aminocyclohexanecarboxylic acid D-Pal=beta-(3-pyridyl)alanine; Tcc=tetrahydrocarbolcnecarboxylic acid Abu=α-aminonormalbutyric acid hArg(Pr)2═N,N′-guanidino-(dipropyl)-homoaxginirne Tic-OH=1,2,3,4 tetrahydroisoquinoline-7-hydroxy-3-carboxylic acid Dip=3,3-diphenylalanine 2-Nal=3(2-naphthylalanine) Tfp=Paratrifluoromethyl phenylalanine Fla=3-(9-Fluorenyl)alanine Flg=9-Fluorenylglycine Cit=Citruline Adp=2,5-diaminoadipic acid Pim=2,6-diaminopimelic acid Sub=2,7-diaminosuberic acid Nle=Norleucine Nva=Norvaline Thz=4-Thiazolylalanine Dpr=Dap=2,3-diaminopropionic acid Pyr=Pyroglutamic acid Tip=1,2,3,4-tetrahydronorharman-3-carboxylic acid Pen=Penicillamine. Other Abbreviations: Fmoc=N-(9-fluorenyl)methoxycarbonyl. The terms “C2-C4-alkenyl” and “C2-C6-alkenyl” as used herein refer to a 2 to 4 to 6 straight- or branched-chain of carbon atoms which contains a carbon-carbon double bond, such as allyl, propenyl, butanol, isoprenyl and the like. The terms “C1-C18-alkyl” as used herein refer to straight or branched chain alkyl radicals having from 1 to 18 carbon atoms including, but not limited to, methyl, ethyl, propyl, isopropyl, butyl, isobutyl, sec-butyl, pentyl, neopentyl hexyl, and the like. The term “C6-C18-aryl” as used herein refers to phenyl or to a “bicyclic carbocyclic” group or “bicyclic carbocycle” having two fused carbocyclic rings, each ring having 5, 6 or 7 carbon atoms, and each ring being fully saturated, partially saturated or aromatic. Bicyclic carbocyclic groups include, but are not limited to, naphthyl, tetrahydronaphthyl, decalin, indanyl, indenyl and the like. The term “C7-C18-arylalkyl” as used herein refers to an aryl group appended to a C1-C4-alkyl radical including, but not limited to, benzyl, phenethyl, naphthylmethyl and the like. The term “bicyclic heterocycle” as used herein refers to a group having two fused rings, one or both of which are heterocyclic rings as defined herein. When both rings are not heterocyclic, the other ring is carbocyclic and is saturated, partially saturated or aromatic, preferably a benzene ring. Bicyclic heterocyclic groups can be unsubstituted or monosubstituted or disubstituted with substituents independently selected from hydroxy, halo, oxo (═O), amino, C1-C4-alkylamino, di-(C1-C4)-alkylamino, C1-C4-alkoxy, thio-C1-C4-alkoxy, carboxy, C1-C4-alkoxycarbonyl, C1-C4-alkyl, C3-C8-cycloalkyl, —OSO3H and halo-C1-C4-alkyl. Examples of bicyclic heterocycles include indole, 5-hydroxyindole, quinoline, isoquinoline, tetrahydroisoquinoline, quinoxaline, benzimidazole, benzofuran, and the like. The term “cyclo-C3-C10-alkyl” as used herein refers to an aliphatic monocyclic of 3 to 10 or bicyclic group having 6 to 10 carbon atoms including, but not limited to, cyclopropyl, cyclobutyl, cyclopentyl, cyclohexyl, cyclooctyl, adamantyl, and the like. The term “halo” or “halogen” as used herein refers to chloro, bromo, iodo or fluoro. The term “halo-C1-C4-alkyl” as used herein refers to a lower alkyl radical in which one to three hydrogen atoms have been replaced by a halogen including, but not limited to, chloromethyl, 2-fluoroethyl, trifluoromethyl and the like. The term “monocyclic heterocyclic group” or “monocyclic heterocycle” as used herein refers to any 3- or 4-membered ring containing a heteroatom selected from oxygen, nitrogen and sulfur, or a 5- or 6-membered ring containing carbon atoms and one, two or three nitrogen atoms; one nitrogen and one sulfur atom; or one nitrogen and one oxygen atom; wherein the 5-membered ring has 0-2 double bonds and the 6-membered ring has 0-3 double bonds; wherein the nitrogen and sulfur heteroatoms may optionally be oxidized; and wherein the nitrogen heteroatom may optionally be quaternized. Heterocycles include, but are not limited to, pyridyl, imidazolyl, furyl, thienyl, pyrazinyl, pyrrolyl, pyrimidyl and the like. Heterocyclics may be unsubstituted or mono- or disubstituted with substituents independently selected from hydroxy, halo, oxo (═O), amino, C1-C4-alkylamino, (C1-C4)2-alkylamino, C1-C4-alkoxy, thio-C1-C4-alkoxy, carboxy, C1-C4-alkoxycarbonyl, C1-C4-alkyl, C3-C8-cycloalkyl, —OSO3H and halo-C1-C4-alkyl. The term “peptide bond” as used herein refers to the chemical bond between carbon and nitrogen in the bivalent group CONH that unites amino acid residues in a peptide. In addition, the above compounds may contain two or more asymmetric carbon atoms and thus can exist as pure diastereomers, mixtures of diastereomers, diastereomeric racemates or mixtures of diastereomeric racemates. As such, the present invention includes within its scope all of the isomeric forms. In keeping with standard peptide nomenclature, J. Biol. Chem., 1969, 243:3557-59, abbreviations for amino acid residues are used herein. It is noted that all amino acid residue sequences are represented herein by formulae whose left to right orientation is in the conventional direction of amino-terminus to carboxy-terminus. Administration The amount of active ingredient that may be combined with the carrier materials to produce a single dosage form will vary depending upon the host treated, the particular treatment and the particular mode of administration. It will be understood, however, that the specific dose level for any particular patient will depend upon a variety of factors including the activity of the specific compound employed, the age, body weight general health, sex, diet, time of administration, rate of excretion, drug combination, and the severity of the particular disease undergoing therapy. However, generally speaking the following guidelines will suffice When an NPY Y4 receptor agonist, such as those of compounds (I-III), is either used alone or in combination with an NPY Y2 receptor agonist, such as those of compounds (IV-V), as an agonist(s) of NPY in a human subject, the total daily dose administered in single or divided doses may be in amounts, for example, from 0.001 to 1000 mg a day and more usually 1 to 1000 mg. Dosage unit compositions may contain such amounts of submultiples thereof to make up the daily dose. The compounds useful in the present inventive method may be administered by any suitable means. One skilled in the art will appreciate that many suitable methods of administering the compounds to an animal in the context of the present invention, in particular a human, are available, and, although more than one route may be used to administer a particular compounds, a particular route of administration may provide a more immediate and more effective reaction than another route. The compositions according to the present invention may be formulated for administration by any suitable route such as the oral, rectal, nasal, topical (dermal) or parenteral administration route. Thus, the composition may be in the form of tablets, capsules, suspensions, emulsions, solutions, injectables, suppositories, sprays, aerosols and in other suitable form. Formulations for oral use include tablets that contain the active ingredient in admixture with non-toxic pharmaceutically acceptable excipients. These excipients may be, for example, inert diluents, such as calcium carbonate, sodium chloride, lactose, calcium phosphate or sodium phosphate; granulating and disintegrating agents, for example, potato starch or alginic acid; binding agents, for example, starch, gelatin or acacia; and lubricating agents, for example, magnesium stearate, stearic acid or talc. Other pharmaceutically acceptable excipients can be colorants, flavoring agents, plasticizers, humectants etc. The tablets may be uncoated or they may be coated by known techniques, optionally to delay disintegration and absorption in the gastrointestinal tract and thereby provide a sustained action over a longer period. For example, a time delay material such as glyceryl monostearate or glyceryl distearate may be employed. Formulations for oral use may also be presented as chewing tablets, or as hard gelatin capsules wherein the active ingredient is mixed with an inert solid diluent, for example, calcium carbonate, calcium phosphate or kaolin, or as soft gelatin capsules wherein the active ingredient is mixed with water or an oil medium, for example, peanut oil, liquid paraffin, or olive oil. Powders, dispersible powders or granules suitable for preparation of an aqueous suspension by addition of water are also convenient dosage forms of the present invention. Formulation as a suspension provide the active ingredient in admixture with a dispersing or wetting agent, suspending agent and one or more preservatives. Suitable dispersing or wetting agents are, for example, naturally-occurring phosphatides, as e.g. lecithin, or condensation products of ethylene oxide with e.g. a fatty acid, a long chain aliphatic alcohol or a partial ester derived from fatty acids and a hexitol or a hexitol anhydrides, for example, polyoxyethylene stearate, polyoxyethylene sorbitol monooleate, polyoxyethylene sorbitan monooleate etc. Suitable suspending agents are, for example, sodium carboxymethylcellulose, methylcellulose, sodium alginate etc. The present agents can also be administered in the form of liposomes. As is known in the art, liposomes are generally derived from phospholipids or other lipid substances. Liposomes are formed by mono- or multi-lamellar hydrated liquid crystals that are dispersed in an aqueous medium. Any non-toxic, physiologically acceptable and metabolizable lipid capable of forming liposomes can be used. The present compositions in liposome form can contain, in addition to the peptides of the present invention, stabilizers, preservatives, excipients, and the like. The preferred lipids are the phospholipids and the phosphatidyl cholines (lecithins), both natural and synthetic. Methods to form liposomes are known in the art. See, for example, Prescott, Ed., Methods in Cell Biology, Volume XIV, Academic Press, New York, N.Y. (1976), p. 33 et seq. The pharmaceutical formulation may also be administered parenterally (intravenous, intramuscular, subcutaneous or the like) in dosage forms or formulations containing conventional, non-toxic pharmaceutically acceptable carriers and adjuvants. The formulation and preparation of such compositions is well-known to those skilled in the art of pharmaceutical formulation. For parenteral use, the pharmaceutical compositions according to the invention may comprise the thermogenic compounds in the form of a sterile injection. To prepare such a composition, the compounds are dissolved or suspended in a parenterally acceptable liquid vehicle. Among acceptable vehicles and solvents that may be employed are water, water adjusted to a suitable pH by addition of an appropriate amount of hydrochloric acid, sodium hydroxide or a suitable buffer, 1,3-butanediol, Ringer's solution and isotonic sodium chloride solution. The aqueous formulation may also contain one or more preservatives, for example, methyl, ethyl or n-propyl p-hydroxybenzoate. For the rectal application, suitable dosage forms for a composition according to the present invention include suppositories (emulsion or suspension type), and rectal gelatin capsules (solutions or suspensions). In a typical suppository formulation, the compounds are combined with an appropriate pharmaceutically acceptable suppository base such as cocoa butter, esterified fatty acids, glycerinated gelatin, and various water-soluble or dispersible bases like polyethylene glycols and polyoxyethylene sorbitan fatty acid esters. Various additives like, for example, enhancers or surfactants, may be incorporated. For the nasal application, typical dosage forms for a composition according to the present invention include nasal sprays and aerosols for inhalation. In a typically nasal formulation, the active ingredients are dissolved or dispersed in a suitable vehicle. The pharmaceutically acceptable vehicles and excipients and optionally other pharmaceutically acceptable materials present in the composition such as diluents, enhances, flavoring agents, preservatives, etc., are all selected in accordance with conventional pharmaceutical practice in a manner understood by the persons skilled in the art of formulating pharmaceuticals. The pharmaceutical compositions according to the invention may also be administered topically on the skin for percutaneous absorption in dosage forms or formulations containing conventionally non-toxic pharmaceutically acceptable carriers and
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