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
Lee, BJ
中科院分区:
生物学3区
文献类型:
--
作者:
Park, S;Park, SH;Lee, BJ

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新型阳离子抗菌肽。从黑斑蛙(Rana nigromaculata)皮肤中分离得到两个新的蛋白质,命名为nigrocin 1和nigrocin 2,并测定了它们的氨基酸序列。这些肽表现出对各种微生物具有不同特异性的广谱抗微生物活性。通过一级结构分析,发现nigrocin 1与brevinin 2具有较高的序列同源性,而nigrocin 2与其他已知的抗菌肽具有较低的序列同源性。为了研究具有独特一级结构的黑曲霉素2的构效关系,进行了圆二色谱(CD)和核磁共振谱(NMR)研究。CD研究表明,在三氟乙醇(TFE)/H_2O溶液、十二烷基硫酸钠(SDS)胶束和十二烷基磷酸胆碱胶束中,黑曲霉素2主要以α-螺旋结构存在。用核磁共振氢谱测定了黑曲霉素2在TFE/H_2O(1:1,v/v)溶液和SDS胶束中的溶液结构。Nigrocin 2由跨越残基3-18的典型两亲性α-螺旋组成,两者均为50%。TFE溶液和SDS胶束。从与其他已知的抗微生物肽的结构比较中,黑曲霉素2可以被分类为含有单个线性两亲性α-螺旋的抗微生物肽家族,该螺旋潜在地破坏膜完整性,这将导致细胞死亡。(C)2001年由Elsevier Science B. V.代表欧洲生物化学学会联合会出版。
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.