Comparison of the proteolytic susceptibilities of homologous L-amino acid, D-amino acid, and N-substituted glycine peptide and peptoid oligomers

摘要: A series of homologous L-amino acid, D-amino and both parallel anti-parallel (retro) sequence N-substituted glycine peptide peptoid oligomers were prepared incubated with a enzymes representative the major classes proteases. Each respective acid containing was readily cleaved by appropriate enzyme, namely Ac-L-ala-L-leu-L-phe-L-ala-L-leu-L-arg-NH2 chymotrypsin, Ac-L-ala-L-ala-L-ala-L-leu-L-phe-L-arg-NH2 elastase, Ac-L-ala-L-phe-L-glu-L-leu-L-ala-L-ala-NH2 papain, Z-L-ala-L-his-L-phe-L-phe-L-arg-L-leu-NH2 pepsin, Ac-L-phe-L-ala-L-arg-L-ala-L-arg-L-asp-NH2 trypsin, Ac-L-ala-L-tyr-Lala-L-phe-OH for carboxypeptidase A. In contrast, equivalent minimally or not at all enzymes. The peptoids represent new class combinatorial diversity lead discovery improved pharmaceutical characteristics relative to peptides. © 1995 Wiley-Liss, Inc.