Structural variations in nisin associated with different membrane mimicking and pH environments

Gary A. Dykes, Robert Hancock, John W. Hastings

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Nisin is a membrane active antimicrobial peptide containing unusual dehydrated amino acid residues. The secondary structure of nisin in aqueous solution, membrane mimicking solvents and at various pH values was investigated using circular dichroism. In aqueous solution nisin is largely randomly coiled. In liposomes and at pH 6 and above, however, the presence of a maximum at 195 nm and a minimum at 190 nm was notable and indicative of β-turn formation in these environments. This change in structure was speculated to result in an increasing unavailability of the site for initial reaction of peptide and membrane at higher pH.

LanguageEnglish
Pages723-727
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume247
Issue number3
DOIs
Publication statusPublished - 29 Jun 1998
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

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Structural variations in nisin associated with different membrane mimicking and pH environments. / Dykes, Gary A.; Hancock, Robert; Hastings, John W.

In: Biochemical and Biophysical Research Communications, Vol. 247, No. 3, 29.06.1998, p. 723-727.

Research output: Contribution to journalArticle

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