Solution and Membrane-Bound Conformational Properties of a Peptide from the First Extracellular Loop of the Angiotensin II AT1 Receptor

  • Shirley Schreier
  • Roberto K. Salinas
  • Cláudio S. Shida
  • Thelma A. Pertinhez
  • Alberto Spisni
  • Clovis R. Nakaie
  • Antonio C. M. Paiva
Part of the American Peptide Symposia book series (APSY, volume 7)

Abstract

The sequence YRWPFGNHL (residues 92–100) is putatively assigned to the first extracellular loop of the angiotensin II AT1A receptor. Residues Trp94 and Gly97 are conserved in nearly 50% of the 1400 rhodopsin-like G protein-coupled receptors [1], and Tyr92 was shown to be important for ligand binding [2]. Homology modeling of the receptor indicates that the WPFG stretch forms a ß-turn. As part of an ongoing study of the conformation and dynamics of synthetic peptides corresponding to extra-membranous domains of the angiotensin II AT1A receptor [3–5], the solution and membrane-bound conformational properties of a synthetic peptide with that sequence (YRWPFGNHL,fEL1) were examined by circular dichroism (CD) and fluorescence.

Keywords

Anisotropy Angiotensin Choline Dodecyl Trifluoro 

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Copyright information

© Springer Science+Business Media Dordrecht 2001

Authors and Affiliations

  • Shirley Schreier
    • 1
  • Roberto K. Salinas
    • 1
  • Cláudio S. Shida
    • 1
  • Thelma A. Pertinhez
    • 1
  • Alberto Spisni
    • 2
  • Clovis R. Nakaie
    • 3
  • Antonio C. M. Paiva
    • 3
  1. 1.Institute of ChemistryUniversity of São PauloSão PauloBrazil
  2. 2.Institute of Biological ChemistryUniversity of ParmaParmaItaly
  3. 3.Department of BiophysicsFederal University of Säo PauloSão PauloBrazil

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