Conformational flexibility of three cytoplasmic segments of the angiotensin II AT1A receptor: A circular dichroism and fluorescence spectroscopy study

Thelma A. Pertinhez, Regina Krybus, Eduardo M. Cilli, Antonio C M Paiva, Clóvis R. Nakaie, Lorella Franzoni, Giorgio Sartor, Alberto Spisni, Shirley Schreier

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

The conformation of three synthetic peptides encompassing the proximal and distal half of the third intracellular loop (Ni3 and Ci3) and a portion of the cytoplasmic tail (fCT) of the angiotensin II AT1A receptor has been studied using circular dischroism and fluorescence spectroscopies. The results show that the conformation of the peptides is modulated in various ways by the environmental conditions (pH, ionic strength and dielectric constant). Indeed, Ni3 and fCT fold into helical structures that possess distinct stability and polarity due to the diverse forces involved: mainly polar interactions in the first case and a combination of polar and hydrophobic interactions in the second. The presence of these various features also produce distinct intermolecular interactions. Ci3, instead, exists as an ensemble of partially folded states in equilibrium. Since the corresponding regions of the angiotensin II AT1A receptor are known to play an important role in the receptor function, due to their ability to undergo conformational changes, these data provide some new clues about their different conformational plasticity.

Original languageEnglish
Pages (from-to)23-35
Number of pages13
JournalJournal of Peptide Science
Volume8
Issue number1
DOIs
Publication statusPublished - 2002

Fingerprint

Circular dichroism spectroscopy
Angiotensin Receptors
Fluorescence Spectrometry
Fluorescence spectroscopy
Circular Dichroism
Conformations
Peptides
Ionic strength
Hydrophobic and Hydrophilic Interactions
Osmolar Concentration
Plasticity
Permittivity

Keywords

  • Angiotensin II AT receptor
  • Circular dichroism
  • Fluorescence
  • G-protein

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry

Cite this

Conformational flexibility of three cytoplasmic segments of the angiotensin II AT1A receptor : A circular dichroism and fluorescence spectroscopy study. / Pertinhez, Thelma A.; Krybus, Regina; Cilli, Eduardo M.; Paiva, Antonio C M; Nakaie, Clóvis R.; Franzoni, Lorella; Sartor, Giorgio; Spisni, Alberto; Schreier, Shirley.

In: Journal of Peptide Science, Vol. 8, No. 1, 2002, p. 23-35.

Research output: Contribution to journalArticle

Pertinhez, TA, Krybus, R, Cilli, EM, Paiva, ACM, Nakaie, CR, Franzoni, L, Sartor, G, Spisni, A & Schreier, S 2002, 'Conformational flexibility of three cytoplasmic segments of the angiotensin II AT1A receptor: A circular dichroism and fluorescence spectroscopy study', Journal of Peptide Science, vol. 8, no. 1, pp. 23-35. https://doi.org/10.1002/psc.364
Pertinhez, Thelma A. ; Krybus, Regina ; Cilli, Eduardo M. ; Paiva, Antonio C M ; Nakaie, Clóvis R. ; Franzoni, Lorella ; Sartor, Giorgio ; Spisni, Alberto ; Schreier, Shirley. / Conformational flexibility of three cytoplasmic segments of the angiotensin II AT1A receptor : A circular dichroism and fluorescence spectroscopy study. In: Journal of Peptide Science. 2002 ; Vol. 8, No. 1. pp. 23-35.
@article{30afe26c04ba40129c46c3215012fa17,
title = "Conformational flexibility of three cytoplasmic segments of the angiotensin II AT1A receptor: A circular dichroism and fluorescence spectroscopy study",
abstract = "The conformation of three synthetic peptides encompassing the proximal and distal half of the third intracellular loop (Ni3 and Ci3) and a portion of the cytoplasmic tail (fCT) of the angiotensin II AT1A receptor has been studied using circular dischroism and fluorescence spectroscopies. The results show that the conformation of the peptides is modulated in various ways by the environmental conditions (pH, ionic strength and dielectric constant). Indeed, Ni3 and fCT fold into helical structures that possess distinct stability and polarity due to the diverse forces involved: mainly polar interactions in the first case and a combination of polar and hydrophobic interactions in the second. The presence of these various features also produce distinct intermolecular interactions. Ci3, instead, exists as an ensemble of partially folded states in equilibrium. Since the corresponding regions of the angiotensin II AT1A receptor are known to play an important role in the receptor function, due to their ability to undergo conformational changes, these data provide some new clues about their different conformational plasticity.",
keywords = "Angiotensin II AT receptor, Circular dichroism, Fluorescence, G-protein",
author = "Pertinhez, {Thelma A.} and Regina Krybus and Cilli, {Eduardo M.} and Paiva, {Antonio C M} and Nakaie, {Cl{\'o}vis R.} and Lorella Franzoni and Giorgio Sartor and Alberto Spisni and Shirley Schreier",
year = "2002",
doi = "10.1002/psc.364",
language = "English",
volume = "8",
pages = "23--35",
journal = "Journal of Peptide Science",
issn = "1075-2617",
publisher = "John Wiley and Sons Ltd",
number = "1",

}

TY - JOUR

T1 - Conformational flexibility of three cytoplasmic segments of the angiotensin II AT1A receptor

T2 - A circular dichroism and fluorescence spectroscopy study

AU - Pertinhez, Thelma A.

AU - Krybus, Regina

AU - Cilli, Eduardo M.

AU - Paiva, Antonio C M

AU - Nakaie, Clóvis R.

AU - Franzoni, Lorella

AU - Sartor, Giorgio

AU - Spisni, Alberto

AU - Schreier, Shirley

PY - 2002

Y1 - 2002

N2 - The conformation of three synthetic peptides encompassing the proximal and distal half of the third intracellular loop (Ni3 and Ci3) and a portion of the cytoplasmic tail (fCT) of the angiotensin II AT1A receptor has been studied using circular dischroism and fluorescence spectroscopies. The results show that the conformation of the peptides is modulated in various ways by the environmental conditions (pH, ionic strength and dielectric constant). Indeed, Ni3 and fCT fold into helical structures that possess distinct stability and polarity due to the diverse forces involved: mainly polar interactions in the first case and a combination of polar and hydrophobic interactions in the second. The presence of these various features also produce distinct intermolecular interactions. Ci3, instead, exists as an ensemble of partially folded states in equilibrium. Since the corresponding regions of the angiotensin II AT1A receptor are known to play an important role in the receptor function, due to their ability to undergo conformational changes, these data provide some new clues about their different conformational plasticity.

AB - The conformation of three synthetic peptides encompassing the proximal and distal half of the third intracellular loop (Ni3 and Ci3) and a portion of the cytoplasmic tail (fCT) of the angiotensin II AT1A receptor has been studied using circular dischroism and fluorescence spectroscopies. The results show that the conformation of the peptides is modulated in various ways by the environmental conditions (pH, ionic strength and dielectric constant). Indeed, Ni3 and fCT fold into helical structures that possess distinct stability and polarity due to the diverse forces involved: mainly polar interactions in the first case and a combination of polar and hydrophobic interactions in the second. The presence of these various features also produce distinct intermolecular interactions. Ci3, instead, exists as an ensemble of partially folded states in equilibrium. Since the corresponding regions of the angiotensin II AT1A receptor are known to play an important role in the receptor function, due to their ability to undergo conformational changes, these data provide some new clues about their different conformational plasticity.

KW - Angiotensin II AT receptor

KW - Circular dichroism

KW - Fluorescence

KW - G-protein

UR - http://www.scopus.com/inward/record.url?scp=0036161308&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036161308&partnerID=8YFLogxK

U2 - 10.1002/psc.364

DO - 10.1002/psc.364

M3 - Article

C2 - 11833541

AN - SCOPUS:0036161308

VL - 8

SP - 23

EP - 35

JO - Journal of Peptide Science

JF - Journal of Peptide Science

SN - 1075-2617

IS - 1

ER -