COMPARISON OF THE PROTEOLYTIC SUSCEPTIBILITIES OF HOMOLOGOUS L-AMINO-ACID, D-AMINO-ACID, AND N-SUBSTITUTED GLYCINE PEPTIDE AND PEPTOID OLIGOMERS
COMPARISON OF THE PROTEOLYTIC SUSCEPTIBILITIES OF HOMOLOGOUS L-AMINO-ACID, D-AMINO-ACID, AND N-SUBSTITUTED GLYCINE PEPTIDE AND PEPTOID OLIGOMERS
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DOI：
10.1002/ddr.430350105
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发表时间：
1995-05-01
影响因子：
3.8
通讯作者：
MOOS, WH
中科院分区：
文献类型：
--
作者：
MILLER, SM;SIMON, RJ;MOOS, WH
A series of homologous L-amino acid, D-amino acid, and both parallel and antiparallel (retro) sequence N-substituted glycine peptide and peptoid oligomers were prepared and incubated with a series of enzymes representative of the major classes of proteases. Each respective L-amino acid containing peptide sequence was readily cleaved by the appropriate enzyme, namely Ac-L-ala-L-leu-L-phe-L-ala-L-leu-L-arg-NH2 by chymotrypsin, Ac-L-ala-L-ala-L-ala-L-leu-L-phe-L-arg-NH2 by elastase, Ac-L-ala-L-phe-L-glu-L-leu-L-ala-L-ala-NH2 by papain, Z-L-ala-L-his-L-phe-L-phe-L-arg-L-leu-NH2 by pepsin, Ac-L-phe-L-ala-L-arg-L-ala-L-arg-L-asp-NH2 by trypsin, and Ac-L-ala-L-tyr-Lala-L-phe-OH for carboxypeptidase A. In contrast, equivalent D-amino acid containing and N-substituted glycine containing oligomers were cleaved minimally or not at all by the respective enzymes. The N-substituted glycine peptoids represent a new class of combinatorial diversity for lead discovery with improved pharmaceutical characteristics relative to L-amino acid containing peptides. (C) 1995 Wiley-Liss, Inc.
