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Folic acid delivery by serum proteins: loading efficacy and protein morphology
P Bourassa1, P Chanphai1, H A Tajmir-Riahi1
1a Département of Chemistry-Biochemistry and Physics , Université du Québec à Trois-Rivières , C. P. 500, Trois-Rivières G9A 5H7 , Québec , Canada.
Abstract:
The loading efficacy of folic acid with serum proteins human serum albumin (HSA), bovine serum albumin (BSA), and beta-lactoglobulin (β-LG) was analyzed and the effect of acid conjugation on protein morphology was determined. Structural analysis showed that folic acid binds HSA, BSA, and β-LG via hydrophilic, hydrophobic, and H-bonding contacts with BSA forming more stable conjugates than HSA and β-LG. Molecular modeling showed the presence of several H-bonding systems, stabilizing acid-protein conjugates. Folic acid conjugation alters protein conformation by major alterations of α-helix and β-sheet. TEM images showed major protein morphological changes inducing protein aggregation upon acid interaction. The results show that serum proteins can deliver folic acid to target molecules.
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