期刊
JOURNAL OF MEDICINAL CHEMISTRY
卷 52, 期 16, 页码 5197-5206出版社
AMER CHEMICAL SOC
DOI: 10.1021/jm900396a
关键词
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资金
- PRIN 2007
- Italian Ministero dell'Istruzione, dell'Universita e della Ricerca
Several aspects of the mechanism of action of Pro-rich antimicrobial peptides, together with their low toxicity ill mammalian cells, make them good candidates for the development of new antibiotic agents. We investigated the effect induced in the insect antimicrobial peptide apidaecin Ib by the replacement of a single arginine/leucine residue witha N-substituted glycine. The resulting peptoid-peptide hybrids are more resistant to proteolysis and devoid of any significant cytotoxic activity, but moving the [NArg]residue from the N- to the C-terminal end of the molecule progressively reduces the antibacterial activity. Cell uptake experiments in E. coli cells suggest that the loss of antibacterial activity of [NArg(17)]apidaecin is a consequence of its inability to translocate into bacterial cells. Conversely, apidaecin and its peptoid-peptide hybrids are able to cross the plasma membrane ill eukaryotic cells and to diffuse in the cytosol, although their translocating ability is far less effective than that of other known cell permeant peptides.
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