Neuroglobin and cellular prion protein (PrP(C)) are expressed in the nervous system and co-localized in the retinal ganglion cell layer. Both proteins do not have an unambiguously assigned function, and it was recently reported that PrP(C) aggregates rapidly in the presence of neuroglobin, whereas it does not aggregate in the presence of myoglobin, another globin with different tissue specificity. Electrostatic complementarity between the unstructured PrP(C) N-terminus and neuroglobin has been proposed to mediate this specific interaction. To verifythis hypothesis experimentally, we have used a combined approach of automated docking and molecular dynamics (MD) studies carried out on short stretches of prion protein (PrP) N-terminus to identify the minimal electrostatically interacting aminoacidic sequences with neuroglobin. Subsequently, we have performed the synthesis of these peptides by solid phase methods, and we tested their interaction with neuroglobin by surface plasmon resonance (SPR). Preliminary results confirm unequivocally the specific interaction between synthetic PrP peptides and neuroglobin suggesting a crucial role of PrP(C) positively charged regions in thisprotein-protein association. Copyright (C) 2011 European Peptide Society and John Wiley & Sons, Ltd.

Neuroglobin-prion protein interaction: what's the function? / Pasquale, Palladino; Giovanni Luca, Scaglione; Alessandro, Arcovito; Maria R., Vitale; Pietro, Amodeo; Vallone, Beatrice; Ettore, Benedetti; Filomena, Rossi; Brunori, Maurizio. - In: JOURNAL OF PEPTIDE SCIENCE. - ISSN 1075-2617. - 17:5(2011), pp. 387-391. (Intervento presentato al convegno 12th Naples Workshop on Bioactive Peptides/2nd Italy-Korea Symposium on Antimicrobial Peptides tenutosi a Naples, ITALY nel JUN 04-07, 2010) [10.1002/psc.1333].

Neuroglobin-prion protein interaction: what's the function?

VALLONE, Beatrice;BRUNORI, Maurizio
2011

Abstract

Neuroglobin and cellular prion protein (PrP(C)) are expressed in the nervous system and co-localized in the retinal ganglion cell layer. Both proteins do not have an unambiguously assigned function, and it was recently reported that PrP(C) aggregates rapidly in the presence of neuroglobin, whereas it does not aggregate in the presence of myoglobin, another globin with different tissue specificity. Electrostatic complementarity between the unstructured PrP(C) N-terminus and neuroglobin has been proposed to mediate this specific interaction. To verifythis hypothesis experimentally, we have used a combined approach of automated docking and molecular dynamics (MD) studies carried out on short stretches of prion protein (PrP) N-terminus to identify the minimal electrostatically interacting aminoacidic sequences with neuroglobin. Subsequently, we have performed the synthesis of these peptides by solid phase methods, and we tested their interaction with neuroglobin by surface plasmon resonance (SPR). Preliminary results confirm unequivocally the specific interaction between synthetic PrP peptides and neuroglobin suggesting a crucial role of PrP(C) positively charged regions in thisprotein-protein association. Copyright (C) 2011 European Peptide Society and John Wiley & Sons, Ltd.
2011
cellular prion protein; nervous system; neuroglobin; peptides synthesis; surface plasmon resonance
01 Pubblicazione su rivista::01a Articolo in rivista
Neuroglobin-prion protein interaction: what's the function? / Pasquale, Palladino; Giovanni Luca, Scaglione; Alessandro, Arcovito; Maria R., Vitale; Pietro, Amodeo; Vallone, Beatrice; Ettore, Benedetti; Filomena, Rossi; Brunori, Maurizio. - In: JOURNAL OF PEPTIDE SCIENCE. - ISSN 1075-2617. - 17:5(2011), pp. 387-391. (Intervento presentato al convegno 12th Naples Workshop on Bioactive Peptides/2nd Italy-Korea Symposium on Antimicrobial Peptides tenutosi a Naples, ITALY nel JUN 04-07, 2010) [10.1002/psc.1333].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/375971
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