期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1984
卷号：81
期号：14
页码：4573-4576
DOI：10.1073/pnas.81.14.4573
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Synthetic di- and oligopeptides are described that contain nucleophilic moieties attached to the carbon of a glycine residue. These peptides are accepted by the peptide transport systems of Escherichia coli (and other microorganisms) and are capable of being hydrolyzed by intracellular peptidases. After liberation of its amino group the -substituted glycine is chemically unstable (although it is stable in peptide form) and decomposes, releasing the nucleophilic moiety. Thus, the combined result of peptide transport and peptidase action is the intracellular release of the nucleophile. Peptides containing glycine residues -substituted with thiophenol, aniline, or phenol are used as models for this type of peptide-assisted entry and their metabolism by E. coli is described. Peptides of this type have broad applicability to the study of microbial physiology and the development of an additional class of antimicrobial agents.
关键词：peptide transport ; portage transport ; oligopeptide permease ; antimicrobial agents ; bacterial transport
