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Titolo:
Helix-stabilizing effects of the pentapeptide KIFMK and its related peptides on the sodium channel inactivation gate peptides
Autore:
Maeda, Y; Nakagawa, T; Kuroda, Y;
Indirizzi:
Kyoto Univ, Grad Sch Pharmaceut Sci, Sakyo Ku, Kyoto 6068501, Japan Kyoto Univ Kyoto Japan 6068501 aceut Sci, Sakyo Ku, Kyoto 6068501, Japan
Titolo Testata:
JOURNAL OF PEPTIDE RESEARCH
fascicolo: 5, volume: 58, anno: 2001,
pagine: 413 - 423
SICI:
1397-002X(200111)58:5<413:HEOTPK>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
HYDROGEN-BONDING INTERACTIONS; PROTEIN SECONDARY STRUCTURE; METHIONINE IFM MOTIF; AMINO-ACIDS; ALPHA-HELICES; CHEMICAL-SHIFT; SIDE-CHAINS; PHENYLALANINE; SPECTROSCOPY; PROPENSITY;
Keywords:
alpha-helix; circular dichroism; H-1 NMR; inactivation gate; KIFMK; sodium channel;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
52
Recensione:
Indirizzi per estratti:
Indirizzo: Kuroda, Y Kyoto Univ, Grad Sch Pharmaceut Sci, Sakyo Ku, Kyoto 6068501, Japan Kyoto Univ Kyoto Japan 6068501 Sakyo Ku, Kyoto 6068501, Japan
Citazione:
Y. Maeda et al., "Helix-stabilizing effects of the pentapeptide KIFMK and its related peptides on the sodium channel inactivation gate peptides", J PEPT RES, 58(5), 2001, pp. 413-423

Abstract

We have previously found by NMR and CD spectroscopic studies that the helical content of the sodium channel inactivation gate-related peptide (Ac-GGQDIFMTEEQK-NH2; MP-1A) in 80% trifluoroethanol solutions was increased by adding a pentapeptide, KIFMK. In order to study in further detail whether thepresence of the IFM motif and the two lysine residues is a prerequisite for stabilizing the helical conformation, we examined interactions between various oligopeptides (RIFMR, KIFMTK, KIQMK, KAFAK, KIIIK) and MP-1A and its related peptides; that is, MP-2A in which Phe was replaced by Gln, MP-1MMA in which Thr was replaced by Met, MP-1TA in which Thr was removed from MP-1A, and MP-1A in which L-Phe was replaced by D-Phe. It was found that the IFM motif was absolutely necessary in both the oligopeptide and the inactivation gate peptide. This finding means that hydrophobic interactions are operative between KIFMK and MP-1A. In contrast, KIFMK destabilized the helical structure of MP1-1MMA, MP-1TA, and MP-1A', showing that the conformation around the IFM motif in the inactivation gate peptides is an important factor. It was concluded that the IFM motif and the two Lys residues are a prerequisite for effectively stabilizing the alpha -helix of MP-1A.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/07/20 alle ore 21:38:38