STRUCTURE, FUNCTION, AND MEMBRANE INTEGRATION OF DEFENSINS
STRUCTURE, FUNCTION, AND MEMBRANE INTEGRATION OF DEFENSINS
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DOI：
10.1016/0959-440x(95)80038-7
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发表时间：
1995-08-01
影响因子：
6.8
通讯作者：
SELSTED, ME
中科院分区：
文献类型：
--
作者：
WHITE, SH;WIMLEY, WC;SELSTED, ME
防御素由一类小阳离子多肽组成，通过膜通透性发挥广谱抗菌活性。它们的主要β-折叠结构由三个二硫键稳定，这使它们有别于其他通常形成两亲性螺旋的抗菌肽。防御素通过静电结合到膜上，随后形成明显的多聚孔。最近的结构和生物物理研究开始提供对渗透过程的洞察。
Defensins comprise a structural class of small cationic peptides that exert broad-spectrum antimicrobial activities through membrane permeabilization. Their predominantly beta-sheet structure, stabilized by three disulfide bonds, distinguishes them from other antimicrobial peptides which typically form amphiphilic helices. Defensins bind to membranes electrostatically and subsequently form apparently multimeric pores. Recent structural and biophysical studies are beginning to provide insights into the process of permeabilization.