Conformational studies of vasopressin and mesotocin using NMR spectroscopy and molecular modelling methods. Part II: studies in the SDS micelle

✍ Scribed by Sylwia Rodziewicz-MotowidŁo; Emilia Sikorska; Marta Oleszczuk; Cezary Czaplewski

• Publisher: John Wiley and Sons
• Year: 2007
• Tongue: English
• Weight: 730 KB
• Volume: 14
• Category: Article
• ISSN: 1075-2617
• DOI: 10.1002/psc.917

✦ Synopsis

Abstract

There is much evidence to support the hypothesis that lipids play a role in the interaction of peptide hormones with their membrane receptors. This interaction through change of peptide conformation can facilitate the entry of the hormone into the microenvironment of the receptor. In the present study we have examined the interaction of vasopressin and mesotocin with a lipid—sodium dodecylsulfate (SDS) micelle—using 2D nuclear magnetic resonance (NMR) and theoretical methods. Solution structures of two hormones in solution with SDS were established using the nuclear Overhauser effect (NOE) and the ^3^J~NHHα~ couplings. The amino acid sequences of these peptides are: c[C^1^‐Y^2^‐F^3^‐Q^4^‐N^5^‐C^6^]‐P^7^‐R^8^‐G^9^‐NH~2~ ([Arg^8^]vasopressin, AVP) and c[C^1^‐Y^2^‐I^3^‐Q^4^‐N^5^‐C^6^]‐P^7^‐I^8^‐G^9^‐NH~2~ (MT). Each of the peptides was found to occur as one stable conformation. AVP adopts the cis configuration on the Cys^1^‐Tyr^2^ peptide bond, a finding not reported so far. The three‐dimensional structures of the two peptides studied were determined by a method that consisted of time‐averaged molecular dynamics in an explicit SDS micelle with the parm99 force field in AMBER8.0 package. All calculated structures of the studied peptides form β‐turns in their cyclic parts. The C‐terminal fragment of MT is bent, whereas that of AVP is extended. Copyright © 2007 European Peptide Society and John Wiley & Sons, Ltd.