Conformation and self-association of the peptide hormone substance P : Fourier-transform infrared spectroscopic study

Download
  1. Get@NRC: Conformation and self-association of the peptide hormone substance P : Fourier-transform infrared spectroscopic study (Opens in a new window)
DOIResolve DOI: http://doi.org/10.1042/bj3010667
AuthorSearch for: ; Search for: ; Search for:
TypeArticle
Journal titleBiochemical Journal
Volume301
IssuePart 3
Pages667670; # of pages: 4
AbstractFourier-transform i.r. (f.t.i.r.) spectroscopy has been applied to the study of the conformational properties of substance P in aqueous solution. Spectra were obtained in the presence of lipid membranes and Ca2+ to assess the role of these factors in induction of the active conformation of the peptide. In aqueous solution substance P was found to be predominantly unstructured at physiological p2H, where the lack of long-range order is probably related to charge repulsion along the peptide chain. However, substance P aggregated in aqueous solution at p2H > 10.0. Little or no induction of secondary structure was seen on addition of the peptide to negatively charged bilayers, suggesting that interaction with a membrane surface does not play an important role in the stabilization of the active conformation of the peptide. In fact, substance P was found to aggregate in the presence of charged lipids, which would tend to hinder rather than enhance interaction with the receptor. We propose a model for the aggregation of substance P at the bilayer surface, based on our studies of the effect of p2H and lipid/peptide ratio on spectra. Addition of Ca2+ had no effect upon the secondary structure of the peptide or on its interactions with membranes.
Publication date
PublisherThe Biochemical Society
LanguageEnglish
AffiliationNational Research Council Canada; NRC Institute for Biodiagnostics
Peer reviewedYes
NRC number308
NPARC number9742390
Export citationExport as RIS
Report a correctionReport a correction
Record identifier1609d6af-b032-4737-8573-e3ab4e6c8e8b
Record created2009-07-17
Record modified2016-12-08
Bookmark and share
  • Share this page with Facebook (Opens in a new window)
  • Share this page with Twitter (Opens in a new window)
  • Share this page with Google+ (Opens in a new window)
  • Share this page with Delicious (Opens in a new window)