Conformational analysis of a potent SSTR3-selective somatostatin analogue by NMR in water solution

Gairí, Margarida; Saiz, Pilar; Madurga, Sergio; Roig, Xavier; Erchegyi, Judit; Koerber, Steven C; Reubi, Jean Claude; Rivier, Jean E; Giralt, Ernest (2006). Conformational analysis of a potent SSTR3-selective somatostatin analogue by NMR in water solution. Journal of Peptide Science, 12(2), pp. 82-91. Chichester: John Wiley & Sons 10.1002/psc.743

Full text not available from this repository. (Request a copy)

The three-dimensional structure of a potent SSTR3-selective analogue of somatostatin, cyclo(3-14)H-Cys(3)-Phe(6)-Tyr(7)-D-Agl(8)(N(beta) Me, 2-naphthoyl)-Lys(9)-Thr(10)-Phe(11)-Cys(14)-OH (des-AA(1, 2, 4, 5, 12, 13)[Tyr(7), D-Agl(8)(N(beta) Me, 2-naphthoyl)]-SRIF) (peptide 1) has been determined by (1)H NMR in water and molecular dynamics (MD) simulations. The peptide exists in two conformational isomers differing mainly by the cis/trans isomerization of the side chain in residue 8. The structure of 1 is compared with the consensus structural motifs of other somatostatin analogues that bind predominantly to SSTR1, SSTR2/SSTR5 and SSTR4 receptors, and to the 3D structure of a non-selective SRIF analogue, cyclo(3-14)H-Cys(3)-Phe(6)-Tyr(7)-D-2Nal(8)-Lys(9)-Thr(10)-Phe(11)-Cys(14)-OH (des-AA(1, 2, 4, 5, 12, 13)[Tyr(7), D-2Nal(8)]-SRIF) (peptide 2). The structural determinant factors that could explain selectivity of peptide 1 for SSTR3 receptors are discussed.

Item Type:

Journal Article (Original Article)

Division/Institute:

04 Faculty of Medicine > Service Sector > Institute of Pathology

UniBE Contributor:

Reubi-Kattenbusch, Jean-Claude

Subjects:

500 Science > 570 Life sciences; biology
600 Technology > 610 Medicine & health

ISSN:

1075-2617

ISBN:

16365912

Publisher:

John Wiley & Sons

Language:

English

Submitter:

Factscience Import

Date Deposited:

04 Oct 2013 14:48

Last Modified:

17 Oct 2019 10:28

Publisher DOI:

10.1002/psc.743

PubMed ID:

16365912

Web of Science ID:

000235422500002

URI:

https://boris.unibe.ch/id/eprint/20301 (FactScience: 3557)

Actions (login required)

Edit item Edit item
Provide Feedback