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Istituto di scienza dell'alimentazione

Torna all'elenco Contributi in rivista anno 2017

Contributo in rivista

Tipo: Articolo in rivista

Titolo: Binding of mycotoxins to proteins involved in neuronal plasticity: a combined in silico/wet investigation

Anno di pubblicazione: 2017

Autori: Scafuri, Bernardina; Varriale, Antonio; Facchiano, Angelo; D'Auria, Sabato; Raggi, Maria Elisabetta; Marabotti, Anna

Affiliazioni autori: CNR; IRCCS Eugenio Medea Bosisio Parini; Univ Salerno

Autori CNR:

  • SABATO D'AURIA
  • ANGELO FACCHIANO
  • BERNARDINA SCAFURI
  • ANTONIO VARRIALE

Lingua: inglese

Abstract: We have applied a combined computational procedure based on inverse and direct docking in order to identify putative protein targets of a panel of mycotoxins and xenobiotic compounds that can contaminate food and that are known to have several detrimental effects on human health. This procedure allowed us to identify a panel of human proteins as possible targets for aflatoxins, gliotoxin, ochratoxin A and deoxynivalenol. Steady-state fluorescence and microscale thermophoresis experiments allowed us to confirm the binding of some of these mycotoxins to acetylcholinesterase and X-linked neuroligin 4, two proteins involved in synapse activity and, particularly for the second protein, neuronal plasticity and development. Considering the possible involvement of X-linked neuroligin 4 in the etiopathogenesis of autism spectrum syndrome, this finding opens up a new avenue to explore the hypothetical role of these xenobiotic compounds in the onset of this pathology.

Lingua abstract: inglese

Pagine totali: 11

Rivista:

Scientific reports Nature Publishing Group
Paese di pubblicazione: Regno Unito
Lingua: inglese
ISSN: 2045-2322

Numero volume: 7

DOI: 10.1038/s41598-017-15148-4

Referee: Sė: Internazionale

Stato della pubblicazione: Published version

Indicizzato da: ISI Web of Science (WOS) [000414810600039]

Parole chiave:

  • myotoxins
  • autism spectrum syndrome
  • molecular docking

Data di accettazione: 16/10/2017

Strutture CNR:

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