Control of cell selectivity of antimicrobial peptides

被引:543
|
作者
Matsuzaki, Katsumi [1 ]
机构
[1] Kyoto Univ, Grad Sch Pharmaceut Sci, Sakyo Ku, Kyoto 6068501, Japan
来源
关键词
Antimicrobial peptide; Cell selectivity; Electrostatic interaction; Hydrophobicity; D-amino acid; Peptpoid; HOST-DEFENSE PEPTIDES; D-AMINO-ACID; LEUCINE-ZIPPER SEQUENCE; MAGAININ; PROTEASE STABILITY; LIPID INTERACTIONS; CATIONIC PEPTIDES; PEPTOID RESIDUES; ACTION MECHANISM; MODEL MEMBRANES;
D O I
10.1016/j.bbamem.2008.09.013
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Antimicrobial peptides (AMPs) are promising novel antibiotics, because they exhibit broad antimicrobial spectra and do not easily induce resistance. For clinical applications, it is important to develop potent AMPs with less toxicity against host cells. This review article summarizes the molecular basis for the cell selectivity (bacteria versus host cells) of AMPs and various attempts to control it, including the optimization of physicochemical parameters of peptides, the introduction Of D-, fluorinated, and unusual amino acids into peptides, the constraining of peptide conformations, and the modification of peptides by polymers. Pros and cons of these approaches are discussed. (C) 2008 Elsevier BY. All rights reserved.
引用
收藏
页码:1687 / 1692
页数:6
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