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Spectroscopic studies of a hydrophobic peptide in membranelike environments
Author(s) -
Gierasch Lila M.,
Lacy Jeffrey E.,
Anderle Gloria,
Lalancette Roger,
Mendelsohn Richard
Publication year - 1983
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360220149
Subject(s) - chemistry , peptide , intramolecular force , vesicle , hydrophobic effect , hydrogen bond , membrane , micelle , stereochemistry , biophysics , biochemistry , organic chemistry , molecule , aqueous solution , biology
A hydrophobic linear peptide has been synthesized and studied over a range of environments using several complementary spectroscopic approaches, including nmr, CD, and vibrational spectroscopies. The sequence of this model peptide, carbobenzoxy‐L‐Pro‐D‐Phe‐D‐Ala‐L‐Pro‐NHCH 3 , was designed such that a small number of “folded” conformations, stabilized by intramolecular hydrogen bonding, would be accessible to it. Additionally, the extremely hydrophobic character of the peptide favors its interactions with hydrophobic regions of a membrane. The conformational impact of the membrane environment on the peptide, and the effect of the peptide on lipid organization have been explored both in micellar media and in vesicles. To facilitate nmr analysis, the peptide has been synthesized with one of the prolines perdeuterated. Results of these studies reveal that the peptide experiences a microenvironment of moderate polarity in micellar media and causes changes in lipid structure in a vesicle that are indicative of a hydrophobic peptide–lipid interaction.