White S H, Wimley W C, Selsted M E
Department of Physiology and Biophysics, University of California, Irvine 92717-4560, USA.
Curr Opin Struct Biol. 1995 Aug;5(4):521-7. doi: 10.1016/0959-440x(95)80038-7.
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.
防御素是一类结构上的小阳离子肽,通过使膜通透发挥广谱抗菌活性。它们主要由β-折叠结构组成,由三个二硫键稳定,这使它们区别于其他通常形成两亲性螺旋的抗菌肽。防御素通过静电作用与膜结合,随后形成明显的多聚体孔。最近的结构和生物物理研究开始为通透过程提供见解。