Biomimetic design is a known approach to developing host molecules for biomedical purposes . In one method, a host molecule, serving as a scaffold, is decorated with peptide chains . The diverse range of amino acids and their strong binding capabilities make them ideal functionalities for modifying CDs in interesting and potentially biologically relevant ways. Although syntheses of β-CDs substituted with amino acids have been reported, they have focused on primary face substitution or non-selective secondary face substitution . Our initial attempts at selective secondary face coupling, with coupling agents HATU, DCC and HBTU, were unsuccessful. However, tetrachloro-N-hydroxyphthalimide tetramethyluronium hexa-fluorophosphate (CITU), a recently developed coupling agent for amide synthesis , in combination with N-methylmorpholine, allowed synthesis of the glycine adduct, 6, in 75 % yields. Again, the reaction required only stirring at room temperature, partial drying, and acetone precipitation, followed by a simple Boc-deprotection step and purification by precipitation. Coupling of bulkier amino acids directly to 3-NH2β-CD remained unsuccessful, though, presumably because of steric hindrance effects, noted above. However, 6 is a good starting point for extension of the peptide chain, as the steric clashes of the polar secondary face are no longer a contributing factor. Accordingly, we have successfully linked Cys and His to the free amino group of 6 (data not shown), leading to β-CD derivatives with Gly-Cys and Gly-His dipeptide substituents.