Molecular mechanism of the inhibition of cytochrome c aggregation by Phe-Gly. (Articolo in rivista)

Type
Label
  • Molecular mechanism of the inhibition of cytochrome c aggregation by Phe-Gly. (Articolo in rivista) (literal)
Anno
  • 2005-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.abb.2004.12.006 (literal)
Alternative label
  • Carmelo La Rosa;a Danilo Milardi;b Emanuela Amato;a Matteo Pappalardo;a Domenico Grasso;a¤ (2005)
    Molecular mechanism of the inhibition of cytochrome c aggregation by Phe-Gly.
    in Archives of biochemistry and biophysics (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Carmelo La Rosa;a Danilo Milardi;b Emanuela Amato;a Matteo Pappalardo;a Domenico Grasso;a¤ (literal)
Pagina inizio
  • 182 (literal)
Pagina fine
  • 189 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 435 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • a Dipartimento di Scienze Chimiche, Universita' di Catania, V.le A. Doria 6, 95125 Catania, Italy b Istituto di Biostrutture e Bioimmagini CNR - Sezione di Catania, Viale A. Doria 6, 95125 Catania, Italy (literal)
Titolo
  • Molecular mechanism of the inhibition of cytochrome c aggregation by Phe-Gly. (literal)
Abstract
  • Experimental and computational studies suggest that few general principles govern protein/protein interactions and aggregation. The knowledge of these rules may be exploited to design peptides that are able to interfere with the self-assembly and aggregation of proteins. This work is aimed to verify the validity of this hypothesis by investigating the interaction of cytochrome e with Phe and Gly amino acids, Ala-His (carnosine), and two water-soluble dipeptides Phe-Gly and Gly-Phe. The combined use of H-1 NMR, MD, and DSC has shown that: (i) at neutral pH, only Phe-Gly is able to prevent the thermally induced aggregation of cytochrome c; (ii) Phe-Gly interacts with Gly45 and Phe46 residues of the protein, either when the protein is in the folded or in the unfolded state; and (iii) the interaction of Phe-Gly with cytochrome c is sequence-dependent. These results support the hypothesis that the basic principles that describe protein aggregation can be used for the design of peptides with antiaggregating properties. (literal)
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