Influences of disulfide connectivity on structure and antimicrobial activity of tachyplesin I

Juan Shi, Lok Yan So, Fangling Chen, Jiazhen Liang, Ho Yin Chow, Kwok Yin Wong, Shengbiao Wan, Tao Jiang, Rilei Yu

Research output: Journal article publicationJournal articleAcademic researchpeer-review

9 Citations (Scopus)


Tachyplesin I is a potent antimicrobial peptide with broad spectrum of antimicrobial activity. It has 2 disulfide bonds and can form 3 disulfide bond isomers. In this study, the structure and antimicrobial activity of 3 tachyplesin I isomers (tachyplesin I, 3C12C, 3C7C) were investigated using molecular dynamic simulations, circular dichroism structural study, as well as antimicrobial activity and hemolysis assay. Our results suggest that in comparison to the native peptide, the 2 isomers (3C12C, 3C7C) have substantial structural and activity variations. The native peptide is in the ribbon conformation, while 3C12C and 3C7C possess remarkably different secondary structures, which are referred as “globular” and “beads” isomers, respectively. The substantially decreased hemolysis effects for these 2 isomers is accompanied by significantly decreased anti-gram-positive bacterial activity.

Original languageEnglish
Article numbere3087
JournalJournal of Peptide Science
Issue number6
Publication statusPublished - Jun 2018


  • antimicrobial activity
  • antimicrobial peptide
  • disulfide connectivity
  • secondary structure
  • tachyplesin I

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Drug Discovery
  • Organic Chemistry


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