The great potential of peptides as therapeutic agents continues to inspire the discovery of new methods for increasing their short half-lives, which are caused by facile proteolytic degradation and rapid renal clearance. A host of structural motifs including peptoids, 2  and / peptides, 3 stapled peptides, hydrogen bond surrogates, AA-peptides, 6 D-peptides, ,-disubstituted amino acids, N-amino peptides, and turn mimics 10 can decrease their susceptibility to proteolysis. Additionally, techniques such as PEGylation, 11 conjugation to albumin or antibody fragments, and anchoring to plasma membranes are effective at slowing renal clearance and/or proteolysis. In spite of these successes, only a modest number of peptide drugs is currently reaching the market. Thus, more strategies for increasing the half-lives of these potential therapeutics are urgently required.