Spectroscopic studies of a hydrophobic peptide in membranelike environments

✍ Scribed by Lila M. Gierasch; Jeffrey E. Lacy; Gloria Anderle; Roger Lalancette; Richard Mendelsohn

• Book ID: 101719595
• Publisher: Wiley (John Wiley & Sons)
• Year: 1983
• Tongue: English
• Weight: 276 KB
• Volume: 22
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.360220149

✦ Synopsis

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-NHCH3, 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.