Folic acid complexes with human and bovine serum albumins.

Abstract:

:The interaction of folic acid with human serum (HSA) and bovine serum albumins (BSA) at physiological conditions, using constant protein concentration and various folic acid contents was investigated. FTIR, UV-visible and fluorescence spectroscopic methods as well as molecular modelling were used to analyse folic acid binding sites, the binding constant and the effect on HSA and BSA stability and conformations. Structural analysis showed that folic acid binds HSA and BSA via both hydrophilic and hydrophobic contacts with overall binding constants of Kfolic acid-HSA=8.1 (±0.5)×10(4)M(-1) and Kfolic acid-BSA=1.0 (±0.3)×10(5)M(-1). The number of bound acid molecules per protein was 1.7 (±0.4) for HSA and 1.5 (±0.3) for BSA complexes. Molecular modelling showed participation of several amino acids in folic acid-protein complexes stabilised by hydrogen bonding network. Folic acid complexation altered protein secondary structure by major reduction of α-helix from 59% (free HSA) to 35% (acid-complex) and 62% (free BSA) to 25% (acid-complex) with an increase in random coil, turn and β-sheet structures indicating protein unfolding. The results suggest that serum albumins might act as carrier proteins for folic acid in delivering it to target molecules.

journal_name

Food Chem

journal_title

Food chemistry

authors

Bourassa P,Hasni I,Tajmir-Riahi HA

doi

10.1016/j.foodchem.2011.05.094

subject

Has Abstract

pub_date

2011-12-01 00:00:00

pages

1148-55

issue

3

eissn

0308-8146

issn

1873-7072

pii

S0308-8146(11)00797-7

journal_volume

129

pub_type

杂志文章