Folic acid delivery by serum proteins: loading efficacy and protein morphology

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.

BSA; HSA; TEM; delivery; folic acid; modeling; morphology; β-LG.