Effect of hydroxypropyl-β-cyclodextrin on the bounding of salazosulfapyridine to human serum albumin

The supramolecular interaction between salazosulfapyridine (SASP) and hydroxypropyl-beta-cyclodextrin (HP-beta-CD), as well as the influence of HP-beta-CD on SASP's binding to human serum albumin (HSA), were investigated. Phase-solubility studies indicate that the HP-beta-CD/SASP inclusion complex was formed at a 1:1 host-guest stoichiometry with high stability constant. The HP-beta-CDISASP complex, which was characterized by various techniques, exhibited markedly improves aqueous solubility of SASP. The binding of SASP with HSA in the presence and absence of HP-beta-CD were investigated. The Stern-Volmer quenching constant and binding constant of SASP with HSA were found to be smaller in the presence of HP-beta-CD. The Forster distance between the donor and the acceptor is altered in the presence of HP-beta-CD. These results exhibited that the HP-beta-CD reduced the quenching and binding of SASP on HSA. Molecular modeling is used to optimize the sites and mode of binding of SASP with HSA. (C) 2016 Elsevier B.V. All rights reserved.