隐窝素-4氨基末端变体与膜之间的定量相互作用。
Quantitative interactions between cryptdin-4 amino terminal variants and membranes.
作者信息
Satchell Donald P, Sheynis Tanya, Kolusheva Sofiya, Cummings Jason, Vanderlick T Kyle, Jelinek Raz, Selsted Michael E, Ouellette Andre J
机构信息
Department of Pathology, College of Medicine, University of California, Irvine, CA 92697-4800, USA.
出版信息
Peptides. 2003 Nov;24(11):1795-805. doi: 10.1016/j.peptides.2003.08.020.
Paneth cells secrete alpha-defensins into the lumen from the base of small intestinal crypts, and cryptdin-4 (Crp4) is the most potent mouse alpha-defensin in vitro. Purified recombinant Crp4 and Crp4 variants with (des-Gly)-, (Gly1Val)-, (Gly1Asp)-, and (Gly1Arg)-substitutions were all bactericidal with Crp4 and (Gly1Arg)-Crp4 being slightly more active than other variants. Bactericidal activities correlated directly with permeabilization of live Escherichia coli, with equilibrium binding to E. coli membrane phospholipid bilayers and vesicles, and with induced graded fluorophore leakage from phospholipid vesicles. The Crp4 peptide N-terminus affects bactericidal activity modestly, apparently by influencing peptide binding to phospholipid bilayers and subsequent permeabilization of target cell membranes.
潘氏细胞从小肠隐窝底部向肠腔分泌α-防御素，隐窝防御素4（Crp4）是体外最有效的小鼠α-防御素。纯化的重组Crp4以及具有（去甘氨酸）-、（甘氨酸1缬氨酸）-、（甘氨酸1天冬氨酸）-和（甘氨酸1精氨酸）-取代的Crp4变体均具有杀菌作用，其中Crp4和（甘氨酸1精氨酸）-Crp4的活性略高于其他变体。杀菌活性与活大肠杆菌的通透性、与大肠杆菌膜磷脂双层和囊泡的平衡结合以及诱导的磷脂囊泡中荧光团分级泄漏直接相关。Crp4肽的N端对杀菌活性有适度影响，显然是通过影响肽与磷脂双层的结合以及随后靶细胞膜的通透性来实现的。
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