Conformational and membrane interaction studies of the antimicrobial peptide alyteserin-1c and its analogue [E4K]alyteserin-1c

Anusha P. Subasinghage, Donal O'Flynn, J. Michael Conlon, Chandralal M. Hewage

Research output: Contribution to journalArticlepeer-review

23 Citations (Scopus)

Abstract

Alyteserin-1c (GLKEIFKAGLGSLVKGIAAHVAS.NH2), first isolated from skin secretions of the midwife toad Alytes obstetricans, shows selective growth-inhibitory activity against Gram-negative bacteria. The structures of alyteserin-1c and its more potent and less haemolytic analogue [E4K]alyteserin-1c were investigated in various solution and membrane mimicking environments by proton NMR spectroscopy and molecular modelling. In aqueous solution, the peptide displays a lack of secondary structure but, in a 2,2,2-trifluoroethanol (TFE-d3)-H2O solvent mixture, the structure is characterised by an extended alpha helix between residues Leu 2 and Val21. Solution structural studies in the membrane mimicking environments, sodium dodecyl sulphate (SDS), dodecylphosphocholine (DPC), and 1,2-dihexanoyl-sn-glycero-3-phosphatidylcholine (DHPC) micelles, indicate that these peptides display an alpha helical structure between residues Lys3 and Val21. Positional studies of the peptides in SDS, DPC and DHPC media show that the N-terminal and central residues lie inside the micelle while C-terminal residues beyond Ala19 do not interact with the micelles.

Original languageEnglish
Pages (from-to)1975-1984
Number of pages10
JournalBiochimica et Biophysica Acta - Biomembranes
Volume1808
Issue number8
DOIs
Publication statusPublished - Aug 2011
Externally publishedYes

Keywords

  • AMP
  • Alyteserin
  • Antimicrobial
  • Molecular modelling
  • NMR
  • Positional studies

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology

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