蜂毒肽
肽
两亲性
抗菌肽
化学
生物化学
天蚕素
肽合成
支原体
膜
组合化学
有机化学
结核分枝杆菌
肺结核
医学
病理
共聚物
聚合物
作者
R. B. Merrifield,E. L. Merrifield,Padmaja Juvvadi,David Andreu,Hans G. Boman
出处
期刊:Novartis Foundation Symposium
日期:2007-09-28
卷期号:: 5-26
被引量:51
标识
DOI:10.1002/9780470514658.ch2
摘要
The cecropins are a group of potent antimicrobial peptides, initially discovered in insects but later found in other animals including mammals. Synthetic peptide chemistry has played an important role in establishing their primary sequences, as well as the steps in the processing of the biosynthetic preprocecropins. Solid-phase peptide synthesis has been the method of choice. Synthetic chimeric peptides have led to more active products and a better understanding of their mode of action. The structural requirements for high activity include a basic amphipathic N-terminus, a short central flexible sequence and a hydrophobic helical C-terminus. Cecropin-melittin hybrids as small as 15 residues are highly active. In planar lipid bilayers the cecropins form pores which pass ions and carry a current under a voltage gradient. Synthetic D-enantiomers of several antibacterial peptides carry the same current as the natural all-L-peptides and are equally active against several test bacteria. Therefore, the activity is not dependent on chiral interactions between the peptides and the lipid bilayers or the bacterial membranes. Recent examination of retro and retroenantio peptides has further defined the limits of the structural requirements of these peptides. Some of the hybrid peptides are active against Plasmodium falciparum and Mycobacterium smegmatis.
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