Abstract：
:The supramolecular interaction between salazosulfapyridine (SASP) and hydroxypropyl-β-cyclodextrin (HP-β-CD), as well as the influence of HP-β-CD on SASP's binding to human serum albumin (HSA), were investigated. Phase-solubility studies indicate that the HP-β-CD/SASP inclusion complex was formed at a 1:1 host-guest stoichiometry with high stability constant. The HP-β-CD/SASP 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-β-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-β-CD. The Förster distance between the donor and the acceptor is altered in the presence of HP-β-CD. These results exhibited that the HP-β-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.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Tang P,Tang B,Wang Q,Xu K,Xiong X,Li Hdoi
10.1016/j.ijbiomac.2016.07.033subject
Has Abstractpub_date
2016-11-01 00:00:00pages
105-115eissn
0141-8130issn
1879-0003pii
S0141-8130(16)30813-3journal_volume
92pub_type
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