pH dependent domain dynamics of HSA controlled by protein based crowding agents

Abstract Here we have investigated the dynamics of domain I of human serum albumin (HSA) in presence of bovine serum albumin and lysozyme as crowders. 6-bromoacetyl-2-dimethylaminonaphthalene (BADAN) covalently attached to cysteine-34 of HSA was used as the solvation probe and changes in its solvation pattern in presence of the crowders were monitored as a function of pH. Lysozyme induced increased retardation of solvation while BSA brought about faster dynamics. Our observations reemphasize the importance of soft interactions even under conditions where repulsive charge-charge interactions dominate, thus reminding us of the enhanced level of complexity that the crowded milieu can possess.