The angiotensin II AT1A receptor belongs to the G-protein coupled receptors (GPCRs). Like other membrane proteins, GPCRs are not easily amenable to direct structure determination by the currently available methods. The peptide encompassing the putative first extracellular loop of AT1A (residues Thr88-Leu100, e1) has been synthesized along with a cyclic model where the linear peptide has been covalently linked to a template designed to keep the distance between the peptide termini as expected in the receptor. The conformational features of the two molecules have been studied using circular dichroism and NMR techniques. The region W94PFG97 forms a type-II β-turn and undergoes a Trp-Pro peptide bond cis-trans isomerization in both peptides confirming that these characteristics are intrinsic to el1. In addition, the presence of the spacer seems to modulate the flexibility of the peptide. Copyright © 2003 European Peptide Society and John Wiley & Sons, Ltd.

Nicastro, G., Peri, F., Franzoni, L., De Chiara, C., Sartor, G., Spisni, A. (2003). Conformational features of a synthetic model of the first extracellular loop of the angiotensin II AT1A receptor. JOURNAL OF PEPTIDE SCIENCE, 9, 229-243.

Conformational features of a synthetic model of the first extracellular loop of the angiotensin II AT1A receptor

PERI, FRANCESCO;
2003

Abstract

The angiotensin II AT1A receptor belongs to the G-protein coupled receptors (GPCRs). Like other membrane proteins, GPCRs are not easily amenable to direct structure determination by the currently available methods. The peptide encompassing the putative first extracellular loop of AT1A (residues Thr88-Leu100, e1) has been synthesized along with a cyclic model where the linear peptide has been covalently linked to a template designed to keep the distance between the peptide termini as expected in the receptor. The conformational features of the two molecules have been studied using circular dichroism and NMR techniques. The region W94PFG97 forms a type-II β-turn and undergoes a Trp-Pro peptide bond cis-trans isomerization in both peptides confirming that these characteristics are intrinsic to el1. In addition, the presence of the spacer seems to modulate the flexibility of the peptide. Copyright © 2003 European Peptide Society and John Wiley & Sons, Ltd.
Articolo in rivista - Articolo scientifico
PEPTIDE chemistry; structural analysis; synthesis; NMR
English
2003
9
229
243
none
Nicastro, G., Peri, F., Franzoni, L., De Chiara, C., Sartor, G., Spisni, A. (2003). Conformational features of a synthetic model of the first extracellular loop of the angiotensin II AT1A receptor. JOURNAL OF PEPTIDE SCIENCE, 9, 229-243.
File in questo prodotto:
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/34268
Citazioni
  • Scopus 10
  • ???jsp.display-item.citation.isi??? 10
Social impact