Apidaecin-type peptides: Biodiversity, structure-function relationships and mode of action

被引:124
作者
Li, Wei-Fen [1 ]
Ma, Guo-Xia
Zhou, Xu-Xia
机构
[1] Zhejiang Univ, Minist Educ Key Lab Mol Anim Nutr, Anim Sci Coll, Hangzhou 310029, Peoples R China
[2] Zhejiang Univ, Dept Chem, Lab Nat & Biochem, Hangzhou 310027, Peoples R China
关键词
apidaecins; biodiversity; structure-function relationships; antibacterial activity; action mechanism;
D O I
10.1016/j.peptides.2006.03.016
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
Apidaecins (apidaecin-type peptides) refer to a series of small, proline-rich (Pro-rich), 18- to 20-residue peptides produced by insects. They are the largest group of Pro-rich antimicrobial peptides (AMPS) known to date. Structurally, apidaecins consist of two regions, the conserved (constant) region, responsible for the general antibacterial capacity, and the variable region, responsible for the antibacterial spectrum. The small, gene-encoded and unmodified apidaecins are predominantly active against many Gram-negative bacteria by special antibacterial mechanisms. The mechanism of action by which apidaecins kill bacteria involves an initial non-specific binding of the peptides to an outer membrane (OM) component. This binding is followed by invasion of the periplasmic space, and by a specific and essentially irreversible combination with a receptor/docking molecule that may be a component of a permease-type transporter system on inner membrane (IM). In the final step, the peptide is translocated into the interior of the cell where it meets its ultimate target. Evidence that apidaecins are non-toxic for human and animal cells is a prerequisite for using them as novel antibiotic drugs. This review presents the biodiversity, structure-function relationships, and mechanism of action of apidaecins. (c) 2006 Elsevier Inc. All rights reserved.
引用
收藏
页码:2350 / 2359
页数:10
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