The use of UV‐visible spectroscopy for the determination of hydrophobic interactions between neuropeptides and membrane model systems

John K. Young, William H. Graham, Debbie J. Beard, Rickey P. Hicks

Research output: Contribution to journalArticle

16 Scopus citations

Abstract

Ultraviolet‐visible spectroscopy has been used as a rapid method to evaluate the hydrophobia interactions between a series of cationic and zwitterionic neuropeptides and dipeptides with the hydrophobia core of two membrane model systems; sodium dodecyl sulfate and lysophosphatidylcholine micelles. If a hydrophobia interaction occurs, a 1−nm bathochromic shift is observed in the uv‐visible spectrum of the aromatic side chains when going from aqueous solution to a micellar solution. The aromatic residues of substance P, bradykinin, and Des‐Arg9 bradykinin all exhibited the 1−nm bathochromic shift in the presence of sodium dodecyl sulfate while those of Met‐enkephalin did not. The opposite effects were observed in the presence of lysophosphatidylcholine micelles. © 1992 John Wiley & Sons, Inc.

Original languageEnglish (US)
Pages (from-to)1061-1064
Number of pages4
JournalBiopolymers
Volume32
Issue number8
DOIs
StatePublished - Aug 1992

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Biomaterials
  • Organic Chemistry

Fingerprint Dive into the research topics of 'The use of UV‐visible spectroscopy for the determination of hydrophobic interactions between neuropeptides and membrane model systems'. Together they form a unique fingerprint.

  • Cite this