Falla T J, Hancock R E
Department of Microbiology and Immunology, University of British Columbia, Vancouver, Canada.
Antimicrob Agents Chemother. 1997 Apr;41(4):771-5. doi: 10.1128/AAC.41.4.771.
A novel cationic peptide, CP-11, based on the structure of the bovine neutrophil peptide indolicidin, was designed to increase the number of positively charged residues, maintain the short length (13 amino acids), and enhance the amphipathicity relative to those of indolicidin. CP-11, and especially its carboxymethylated derivative, CP-11C, demonstrated improved activity against gram-negative bacteria and Candida albicans, while it maintained the activity of indolicidin against staphylococci and demonstrated a reduced ability to lyse erythrocytes. In Escherichia coli, CP-11 was better able than indolicidin to permeabilize both the outer membrane, as indicated by the enhancement of uptake of 1-N-phenylnaphthylamine, and the inner membrane, as determined by the unmasking of cytoplasmic beta-galactosidase, providing an explanation for its improved activity.
基于牛中性粒细胞肽吲哚杀菌素的结构设计了一种新型阳离子肽CP-11，旨在增加带正电荷残基的数量，保持较短的长度（13个氨基酸），并相对于吲哚杀菌素增强两亲性。CP-11，尤其是其羧甲基化衍生物CP-11C，对革兰氏阴性菌和白色念珠菌表现出更高的活性，同时保持了吲哚杀菌素对葡萄球菌的活性，并表现出较低的红细胞裂解能力。在大肠杆菌中，CP-11比吲哚杀菌素更能使外膜通透性增加（通过1-N-苯基萘胺摄取的增强表明），也能使内膜通透性增加（通过细胞质β-半乳糖苷酶的暴露确定），这为其活性提高提供了解释。
