Solution structure of a designed amphipathic antimicrobial synthetic peptide, PGAa

Eunmi Hong, Pan Young Jeong, Jin Won Jung, Yangmee Kim, Chaejoon Cheong, Young Ki Paik, Weontae Lee

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)


A designed peptide, PGAa showed an excellent anti-fungal activity as well as an efficient bactericidal activity toward gram-positive, especially in the pathogenic yeast Candida albicans 28838. The solution structures of PGAa have been determined both in 40% TFE/water solution and DPC micelle by CD and NMR spectroscopy. Based on NOEs, vicinal coupling constants, backbone amide exchange rates, and chemical shift indices, PGAa formed a long amphipathic α-helical conformation in both TFE and DPC micelle environments, spanning the residues Ile2-Ala19 in TFE and Lys5-Ala19 in DPC micelle, respectively. Solution structures suggested that the hydrophobic residues would interact with the fatty acyl chains of the lipid bilayer, while the positively charged side-chains exposed to aqueous environments. Therefore, we conclude that the ≃-helical structure as well as the highly amphiphatic nature of PGAa peptide may play a critical role in its antimicrobial activity as well as selectivities in different species. (C) 2000 Academic Press.

Original languageEnglish
Pages (from-to)1278-1285
Number of pages8
JournalBiochemical and Biophysical Research Communications
Issue number3
Publication statusPublished - 2000 Oct 5

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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