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• W2913612268 abstract "Streptozocin (STZ) is a broad range antibiotic, highly genotoxic, antineoplastic and hyperglycemic. HSA is the most abundant protein in physiology and it binds to almost all exogenic and endogenic ligands, including drugs. STZ-induced fluorescence quenching of HSA has been done at pH 7.4, pH 3.5 and at pH 7.4 with 4.5 M urea at temperatures 286 K, 291 K, and 306 K. Ksv found to be 103 M−1, binding constant 1.5X103M−1 and binding sites ~1. But, Ksv for HSA and glucopyranose interaction was found lesser than that of HSA-STZ binding. Binding of STZ/glucopyranose on HSA seems to result in complex formation as calculated Kq > 1010 M−1 s−1. The number of binding sites, binding constants, and binding energies were increased with temperature. The ΔG0, ΔH0, and ΔS0 for HSA-STZ interaction were found to be −17.7 × 103 J·mol−1; 2.34 × 105 J·mol−1 and 841 JK−1 mol−1 respectively at pH 7.4 and 291 K. The comparative bindings of N, F and I states of HSA with STZ and their molecular docking analyses indicate that IIIA-B junction (i.e., inter-helix h6DOM3-h7DOM3) is the probable binding site, a locus close to fatty acid binding site-5. These results could be useful for therapeutic and analytical exploitation of STZ, as albumin used as the vehicle for drug delivery." @default.
• W2913612268 created "2019-02-21" @default.
• W2913612268 creator A5011745113 @default.
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• W2913612268 date "2019-05-01" @default.
• W2913612268 modified "2023-09-25" @default.
• W2913612268 title "Streptozocin; a GLUT2 binding drug, interacts with human serum albumin at loci h6DOM3-h7DOM3" @default.
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• W2913612268 doi "https://doi.org/10.1016/j.ijbiomac.2019.01.217" @default.
• W2913612268 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30716368" @default.
• W2913612268 hasPublicationYear "2019" @default.
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