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

  1. Silva, Mafalda
  2. Sousa, Sérgio F.
  3. Teixeira, Natércia
  4. García-Estévez, Ignacio
  5. Fonseca, Fátima
  6. de Freitas, Victor
  7. Soares, Susana
  8. Ferrer-Galego, Raúl
  9. Mateus, Nuno
  10. Brás, Natércia F.
  11. Brandão, Elsa
  12. Ferreira-da-Silva, Frederico
Revue:
Food Chemistry

ISSN: 0308-8146

Année de publication: 2018

Volumen: 243

Pages: 175-185

Type: Article

DOI: 10.1016/J.FOODCHEM.2017.09.063 GOOGLE SCHOLAR lock_openAccès ouvert editor

D'autres publications dans: Food Chemistry

Résumé

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.