Helicity propensity and interaction of synthetic peptides from heptad-repeat domains of herpes simplex virus 1 glycoprotein H: A circular dichroism study

Barbara Sanavio, Angela Piccoli, Tatiana Gianni, Carlo Bertucci

Research output: Contribution to journalArticlepeer-review

Abstract

The secondary structure of two synthetic peptides from heptad-repeat domains of herpes simplex virus 1 glycoprotein H was determined by circular dichroism. In particular, the propensity of these peptides to assume an ordered structure was investigated upon by changing the solvent's polarity and the temperature. A reduction of solvent polarity led to a significant increase in the α-helix content in the case of HR1, whereas only a slight change in the secondary structure was observed in the case of HR2. In both cases the conformational change followed a two-state transition model. The interaction of the peptides was monitored by the conformational change in the mixture with respect to the single peptides. However, formation of the complex did not significantly enhance thermal stability. A reliable estimation of the secondary structure was obtained by optimising the experimental conditions to collect CD data down to 180 nm, and by comparing the structure data yielded by different software packages.

Original languageEnglish
Pages (from-to)781-791
Number of pages11
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Volume1774
Issue number7
DOIs
Publication statusPublished - Jul 2007

Keywords

  • Circular dichroism
  • Peptide folding
  • Peptide-peptide complexes
  • Secondary structure estimation
  • Thermal denaturation

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Genetics

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