Study of human salivary proline-rich proteins interaction with food tannins

• Type: Article in International Scientific Journal
• Date: 2018

Authors

Susana Soares (Author) FCUP; Garcia Estevez, I (Author) Other; Ferrer Galego, R (Author) Other; Natercia F Bras (Author) FCUP; Brandao, E (Author) Other; Silva, M (Author) Other; Teixeira, N (Author) Other; Fonseca, F (Author) Other; Sergio Filipe Sousa (Author) FCUP; Ferreira da Silva, F (Author) Other; Nuno Mateus (Author) FCUP; Victor de Freitas (Author) FCUP

Journal

Title: Food Chemistry

Vol. 243

Pages: 175-185

ISSN: 0308-8146

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 41 Citations

Scopus - 44 Citations

Other information

Authenticus ID: P-00N-39R

DOI: 10.1016/j.foodchem.2017.09.063

Abstract (EN): In this work, saturation transfer difference-NMR, isothermal microcalorimetry and molecular dynamics simulations have been used to study the individual interactions between basic, glycosylated and acidic proline-rich proteins (bPRPS, gPRPs, aPRPs) and P-B peptide with some representative food tannins [procyanidin B2, procyanidin B2 3'-O-gallate (B2g) and procyanidin trimer (catechin-4-8-catechin-4-8-catechin)]. Results showed that P-B peptide was in general the salivary protein (SP) with higher affinity whereas aPRPs showed lower affinity to the studied procyanidins. Moreover, B2g was the procyanidin with higher affinity for all SP. Hydrophobic and hydrogen bonds were present in all interactions but the major driving force depended on the procyanidin-SP pair. Furthermore, proline clusters or residues in their vicinity were identified as the probable sites of proteins for interaction with procyanidins. For bPRP and aPRP a significant change to less extended conformations was observed, while P-B peptide did not display any structural rearrangement upon procyanidins binding.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 11