http://www.cnr.it/ontology/cnr/individuo/prodotto/ID169453

Conformational features of human melanin-concentrating hormone: an NMR and computational analysis (Articolo in rivista)

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Conformational features of human melanin-concentrating hormone: an NMR and computational analysis (Articolo in rivista) (literal)

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Vitale, Rosa Maria; Zaccaro, Laura; Di Blasio, Benedetto; Fattorusso, Roberto; Isernia, Carla; Amodeo, Pietro; Pedone, Carlo; Saviano, Michele (2003)
Conformational features of human melanin-concentrating hormone: an NMR and computational analysis
in ChemBioChem (Print)
(literal)

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Vitale, Rosa Maria; Zaccaro, Laura; Di Blasio, Benedetto; Fattorusso, Roberto; Isernia, Carla; Amodeo, Pietro; Pedone, Carlo; Saviano, Michele (literal)

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Lavoro scientifico su rivista internazionale con la caratterizzazione conformazionale di un peptide implicato nella regolazione della fame. (literal)

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Istituto di Biostrutture e Bioimmagini CNR Napoli Istituto di chimica biomolecolare, Pozzuoli Napoli Dipartimento di Scienze Ambientali Seconda Universita di Napoli, Caserta (literal)

Titolo

Conformational features of human melanin-concentrating hormone: an NMR and computational analysis (literal)

Abstract

The conformational features of human melanin-concentrating hormone (hMCH) [Asp1-Phe2-Asp3-Met4-Leu5-Arg6-cyclo(S[bond]S)(Cys7-Met8-Leu9-Gly10-Arg11-Val12-Tyr13-Arg14-Pro15-Cys16)-Trp17-Gln18-Val19], in water and in a CD(3)CN/H(2)O (1:1 v/v) mixture at 298 K, have been determined by NMR spectroscopy followed by simulated annealing and molecular dynamics analyses to identify conformer populations. Backbone clustering analysis of NMR-spectroscopy-derived structures in the 7-16 peptide region led to the identification of a single representative structure in each solvent. Both root mean square deviation clustering and secondary structure analysis of the final conformers in both solvents show substantial convergence of most conformers into a single fold in the 4-17 region, with a limited variability around Gly10 and Tyr13 on going from CD(3)CN/H(2)O to pure water. The main feature deduced from the analysis of secondary structures is the occurrence of an N-terminal alpha helix of variable length, which spans an overall residue range of 2-9. A comparative analysis in the two solvents highlights that these structures are substantially different from that reported in the literature for the cyclic MCH(5-14) subunit of salmon MCH, which was used to perform a molecular characterization of the MCH/receptor complex. Our conformational data call for a critical revision of the proposed MCH/receptor complex model. (literal)

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