Conjugation of citric acid and gallic acid with serum albumins: Acid binding sites and protein conformation

摘要: Abstract We studied the effect of citric acid and gallic on solution structures bovine serum albumin (BSA) human albumins (HSA) at pH 7.2. Thermodynamic parameters ∆H0–13.30 to −5.60 (kJ mol−1), ∆S0 27.35 2.40 (J mol−1 K−1) ∆G0–14.80 −13.75 (kJ mol−1) showed that binds protein via ionic contacts with forming stronger conjugates. Different amino acids are involved in complexation, while HSA more stable complexes. Protein conformation was altered major reduction α-helix an increase random coil turn structures, indicating a partial destabilization.