Elongation of the BH8 β-hairpin peptide: Electrostatic interactions in β-hairpin formation and stability

Marina Ramírez-Alvarado, Francisco J. Blanco, Luis Serrano

Research output: Contribution to journalArticle

44 Scopus citations

Abstract

An elongated version of the de novo designed β-hairpin peptide, BH8, has allowed us to gain insight into the role of electrostatic interactions in β-hairpin stability. A Lys-Glu electrostatic pair has been introduced by adding a residue at the beginning and at the end of the N-terminal and C-terminal strands, respectively, of the β-hairpin structure, in both orientations. The two resulting peptides and controls having Ala residues at these positions and different combinations of Ala with Lys, or Glu residues, have been analyzed by nuclear magnetic resonance (NMR), under different pH and ionic strength conditions. All of the NMR parameters, in particular the conformational shift analysis of Cα protons and the coupling constants, 3JHNα, correlate well and the population estimates are in reasonable agreement among the different methods used. In the most structured peptides, we find an extension of the β-hairpin structure comprising the two extra residues. Analysis of the pH and salt dependence shows that ionic pairs contribute to β-hairpin stability. The interaction is electrostatic in nature and can be screened by salt. There is also an important salt-independent contribution of negatively charged groups to the stability of this family of β-hairpin peptides.

Original languageEnglish (US)
Pages (from-to)1381-1392
Number of pages12
JournalProtein Science
Volume10
Issue number7
DOIs
StatePublished - Jul 4 2001

Keywords

  • NMR
  • Peptides
  • Protein folding
  • Secondary structure
  • β-hairpin

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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