Calorimetric, spectroscopic and computational investigation of morin binding effect on bovine serum albumin stability

Impact of Sinapic Acid on Bovine Serum Albumin Thermal Stability

“…Previous calorimetric studies [24] concerning BSA thermal stability in phosphate buffer evidenced only the endothermal denaturation process. That was confirmed by our previous contributions [25][26][27]. In other words, the phosphate buffer covers the exothermal calorimetric signature of the aggregation process; although, the later takes place in the temperature range investigated.…”

“…The stabilization effect on the secondary structure of the protein, observed for both 1:1 and 10:1 SA:BSA molar ratios, could be correlated with µDSC data, where T d increases in the presence of the ligand. Similar results were obtained for the interaction of morin [25], caffeic acid [26], and caffeoylquinic acids [36] with BSA.…”

“…A significant impact was observed for a 10:1 SA:BSA molar ratio, pointing to the stabilization effect of the excess free ligand. A similar influence was obtained for morin, a polyphenol that belongs to the flavanol class of flavonoids, in interaction with BSA [25]. The stabilization of protein structure could be generated by the electrostatic attraction between the negatively charged SA and the positively charged amino acid residues from the protein binding site, as observed by our group for the caffeic acid interaction with BSA [26].…”

Isothermal titration calorimetry investigation of the interactions between vitamin B6-derived hydrazones and bovine and human serum albumin

“…The binding process between small molecules and proteins in solution may involve different interactions strictly related to their structural properties. Van der Waals forces, electrostatic and hydrophobic interactions are usually the main driving forces that occur in the recognition process [31][32][33][34]. Due to the specific structures of both hydrazones and serum albumins examined in this work, the binding events may be mainly attributed to (i) hydrophobic interactions between the aromatic moiety of the hydrazones and the hydrophobic cavity of the protein, (ii) electrostatic interactions between the phosphate group of the hydrazones and the polar amino groups of BSA/HSA, (iii) hydrogen bonding between the hydroxyl and phosphate groups of the hydrazones and the amino and hydroxyl groups of BSA/HSA and (iv) desolvation and/or structural re-arrangement of both the hydrazone and the protein upon complexation [35][36][37].…”