Under specific physico-chemical conditionsβ-lactoglobulin is seen to formfibrils structurally highly similar tothose that are formed by the amyloid-like proteins associated with neurodegenerative disorders, such asAlzheimer and Parkinson diseases. In the present study we provide insights on the possible role that the dietaryflavonoid (−)-epicatechin plays onβ-lactoglobulinfibril formation. Fibril formation is induced by keepingβ-lactoglobulin solutions at pH 2.0 and at a temperature of 80 °C for 24 h. Atomic Force Microscopy measurementssuggest that, by adding (−)-epicatechin in the solution,fibrils density is visibly lowered. This last observation isconfirmed by Fluorescence Correlation Spectroscopy experiments. With the use of Fourier Transform IR spectros-copy we monitored the relative abundances of the secondary structures components during the heating process.We observed that in the presence of (−)-epicatechin the spectral-weight exchange between different secondarystructures is partially inhibited. Molecular Dynamics simulations have been able to provide an atomistic explana-tion of this experimental observation, showing that (−)-epicatechin interacts withβ-lactoglobulin mainly viathe residues that, normally in the absence of (−)-epicatechin, are involved inβ-sheet formation. Unveilingthis molecular mechanism is an important step in the process of identifying suitable molecules apt atfinelytuningfibril formation like it is desirable to do in food industry applications

Role of dietary antioxidant (-)-epicatechin in the development of β-lactoglobulin fibrils / Carbonaro, M.; Di Venere, A.; Filabozzi, A.; Maselli, Paola; Minicozzi, V; Morante, S.; Nicolai, E.; Nucara, Alessandro; Placidi, E.; Stellato, F.. - In: BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS. - ISSN 1570-9639. - STAMPA. - 1864:7(2016), pp. 766-772. [10.1016/j.bbapap.2016.03.017]

Role of dietary antioxidant (-)-epicatechin in the development of β-lactoglobulin fibrils

MASELLI, Paola;NUCARA, Alessandro;Placidi, E.;
2016

Abstract

Under specific physico-chemical conditionsβ-lactoglobulin is seen to formfibrils structurally highly similar tothose that are formed by the amyloid-like proteins associated with neurodegenerative disorders, such asAlzheimer and Parkinson diseases. In the present study we provide insights on the possible role that the dietaryflavonoid (−)-epicatechin plays onβ-lactoglobulinfibril formation. Fibril formation is induced by keepingβ-lactoglobulin solutions at pH 2.0 and at a temperature of 80 °C for 24 h. Atomic Force Microscopy measurementssuggest that, by adding (−)-epicatechin in the solution,fibrils density is visibly lowered. This last observation isconfirmed by Fluorescence Correlation Spectroscopy experiments. With the use of Fourier Transform IR spectros-copy we monitored the relative abundances of the secondary structures components during the heating process.We observed that in the presence of (−)-epicatechin the spectral-weight exchange between different secondarystructures is partially inhibited. Molecular Dynamics simulations have been able to provide an atomistic explana-tion of this experimental observation, showing that (−)-epicatechin interacts withβ-lactoglobulin mainly viathe residues that, normally in the absence of (−)-epicatechin, are involved inβ-sheet formation. Unveilingthis molecular mechanism is an important step in the process of identifying suitable molecules apt atfinelytuningfibril formation like it is desirable to do in food industry applications
2016
(-)-Epicatechin; Aggregates; Fibrils; β-Lactoglobulin; Biochemistry; Biophysics; Analytical Chemistry; Molecular Biology
01 Pubblicazione su rivista::01a Articolo in rivista
Role of dietary antioxidant (-)-epicatechin in the development of β-lactoglobulin fibrils / Carbonaro, M.; Di Venere, A.; Filabozzi, A.; Maselli, Paola; Minicozzi, V; Morante, S.; Nicolai, E.; Nucara, Alessandro; Placidi, E.; Stellato, F.. - In: BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS. - ISSN 1570-9639. - STAMPA. - 1864:7(2016), pp. 766-772. [10.1016/j.bbapap.2016.03.017]
File allegati a questo prodotto
File Dimensione Formato  
Carbonaro_Role_2016.pdf

solo gestori archivio

Note: articolo fibrille 2016 progetto eccellenza
Tipologia: Documento in Post-print (versione successiva alla peer review e accettata per la pubblicazione)
Licenza: Tutti i diritti riservati (All rights reserved)
Dimensione 447.51 kB
Formato Adobe PDF
447.51 kB Adobe PDF   Contatta l'autore

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/875633
Citazioni
  • ???jsp.display-item.citation.pmc??? 3
  • Scopus 18
  • ???jsp.display-item.citation.isi??? 18
social impact