Structural study of novel antimicrobial peptides, nigrocins, isolated from Rana nigromaculata

Sangho Park, Sang Ho Park, Hee Chul Ahn, Sunkyu Kim, Sunny S. Kim, Byeong Jae Lee, Bong Jin Lee

Research output: Contribution to journalArticlepeer-review

87 Scopus citations

Abstract

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 α-helical structure in trifluoroethanol (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 α-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 α-helix that potentially disrupts membrane integrity, which would result in cell death.

Original languageEnglish
Pages (from-to)95-100
Number of pages6
JournalFEBS Letters
Volume507
Issue number1
DOIs
StatePublished - 19 Oct 2001

Keywords

  • Antimicrobial peptide
  • Circular dichroism
  • Nuclear magnetic resonance
  • Solution structure

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