Structural study of novel antimicrobial peptides, nigrocins, isolated from Rana nigromaculata
Structural study of novel antimicrobial peptides, nigrocins, isolated from Rana nigromaculata
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DOI:
10.1016/s0014-5793(01)02956-8
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发表时间:
2001-10-19
期刊:
影响因子:
3.5
通讯作者:
Lee, BJ
中科院分区:
文献类型:
--
作者:
Park, S;Park, SH;Lee, BJ
Novel cationic antimicrobial peptides. named nigrocin 1 and 2, were isolated from the skin of Rana nigromaculata and their amino acid sequences were determined. These peptides manifested a broad spectrum of antimicrobial activity against various microorganisms with different specificity. By primary structural analysis, it was revealed that nigrocin 1 has high sequence homology with brevinin 2 but nigrocin 2 has low sequence homology with any other known antimicrobial peptides. To investigate the structure-activity relationship of nigrocin 2, which has a unique primary structure, circular dichroism (CD) and homonuclear nuclear magnetic resonance spectroscopy (NMR) studies were performed. CD investigation revealed that nigrocin 2 adopts mainly an cc-helical structure in trifluoro,ethanol (TFE)/H2O Solution, sodium dodecyl sulfate (SDS) micelles, and dodecylphosphocholine micelles. The solution structures of nigrocin 2 in TFE/H2O (1:1, v/v) solution and in SDS micelles were determined by homonuclear NMR. Nigrocin 2 consists of a typical amphipathic a-helix spanning residues 3-18 in both 50%. TFE solution and SDS micelles. From the structural comparison of nigrocin 2 with other known antimicrobial peptides, nigrocin 2 could be classified into the family of antimicrobial peptides containing a single linear amphipathic a-helix that potentially disrupts membrane integrity, which would result in cell death. (C) 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.