title: Modulation of accessibility of subdomain IB in the pH-dependent interaction of bovine serum albumin with Cochineal Red A: a combined view from spectroscopy and docking simulations.
abstract: Our recent report on the binding of Cochineal Red A, a food dye, with HSA and BSA at pH 7.4 has revealed that electrostatic forces is the principal cause of interaction. In that study issues relating to complications arising out of modulation of dye binding affinity of BSA with pH had not been explored. Here we have further explored the interaction of Cochineal Red A with BSA in pH range 4.8-7.8. Surprisingly, this system behaves differently in the texture of interaction pattern at two extremes of studied pH range, unlike HSA. Importantly, the charge on the amino acid side chains in the binding pocket is likely to play a significant role.
authors.affiliation: Department of Chemistry, Indian Institute of Technology, Kharagpur 721302, India.
authors.forename: Priyanka
authors.initials: P
authors.lastname: Bolel
authors.forename: Niharendu
authors.initials: N
authors.lastname: Mahapatra
authors.forename: Shubhashis
authors.initials: S
authors.lastname: Datta
authors.forename: Mintu
authors.initials: M
authors.lastname: Halder
mesh_terms: D000818:Animals; D001391:Azo Compounds / Q000737:chemistry*; D001665:Binding Sites; D002417:Cattle; D002942:Circular Dichroism; D005503:Food Additives / Q000737:chemistry; D006801:Humans; D006863:Hydrogen-Ion Concentration; D062105:Molecular Docking Simulation; D015394:Molecular Structure; D009282:Naphthalenesulfonates; D012709:Serum Albumin / Q000737:chemistry*; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D055672:Static Electricity
chemical_list: D001391:Azo Compounds; D005503:Food Additives; D009282:Naphthalenesulfonates; D012709:Serum Albumin; D012710:Serum Albumin, Bovine; C576297:ponceau 4R