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Titolo:
Conformationally restricted PACAP27 analogues incorporating type II/II ' IBTM beta-turn mimetics. Synthesis, NMR structure determination, and bindingaffinity
Autore:
Gonzalez-Muniz, R; Martin-Martinez, M; Granata, C; de Oliveira, E; Santiveri, CM; Gonzalez, C; Frechilla, D; Herranz, R; Garcia-Lopez, MT; Del Rio, J; Jimenez, MA; Andreu, D;
Indirizzi:
CSIC, Inst Quim Med, E-28006 Madrid, Spain CSIC Madrid Spain E-28006CSIC, Inst Quim Med, E-28006 Madrid, Spain Univ Barcelona, Dept Quim Organ, E-08028 Barcelona, Spain Univ Barcelona Barcelona Spain E-08028 m Organ, E-08028 Barcelona, Spain CSIC, Inst Estructura Mat, E-28006 Madrid, Spain CSIC Madrid Spain E-28006 IC, Inst Estructura Mat, E-28006 Madrid, Spain Univ Navarra, Dept Farmacol, Pamplona 31008, Spain Univ Navarra PamplonaSpain 31008 , Dept Farmacol, Pamplona 31008, Spain
Titolo Testata:
BIOORGANIC & MEDICINAL CHEMISTRY
fascicolo: 12, volume: 9, anno: 2001,
pagine: 3173 - 3183
SICI:
0968-0896(200112)9:12<3173:CRPAIT>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
CYCLASE-ACTIVATING POLYPEPTIDE; VASOACTIVE-INTESTINAL-PEPTIDE; NUCLEAR-MAGNETIC-RESONANCE; CHEMICAL-SHIFTS; SECONDARY STRUCTURE; MOLECULAR-DYNAMICS; RECEPTOR AGONIST; VIP1 RECEPTOR; RAT-BRAIN; PITUITARY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
55
Recensione:
Indirizzi per estratti:
Indirizzo: Gonzalez-Muniz, R CSIC, Inst Quim Med, Juan Cierva 3, E-28006 Madrid, Spain CSIC Juan Cierva 3 Madrid Spain E-28006 6 Madrid, Spain
Citazione:
R. Gonzalez-Muniz et al., "Conformationally restricted PACAP27 analogues incorporating type II/II ' IBTM beta-turn mimetics. Synthesis, NMR structure determination, and bindingaffinity", BIO MED CH, 9(12), 2001, pp. 3173-3183

Abstract

To probe the importance of a proposed U-turn within residues S9-R12 of PACAP for recognition by VIP/PACAP receptors, compounds 1 and 2, two conformationally restricted analogues of PACAP27 incorporating respectively (S)- or (R)-IBTM as type II or II' beta -turn dipeptide mimetic at the Y10-S11 position, were synthesized. According to H-1 NMR conformational analyses in aqueous solution and 30% TFE, both PACAP-27 and the [S-IBTM10,11]PACAP27 analogue I adopt similar ordered structures. PACAP27 shows Lin N-terminal disordered region (residues H1-F6) and an alpha -helical conformation within segment T7-L27. For residues S9-R12, our data seem more compatible with a segment of the alpha -helix than with the beta -turn previously proposed for this fragment. In compound 1 the alpha -helix, also spanning T7-L27 residues, appears slightly distorted at the N-terminus relative to the native peptide. Although this distortion could lead to the marked decrease in binding affinity of this compound at the VIP/PACAP receptors, the lack of the Y10 sidechain in analogues 1 and 2 could also significantly affect the binding of these compounds. (C) 2001 Elsevier Science Ltd. All rights reserved.

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Documento generato il 30/05/20 alle ore 15:11:44