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• W1965536281 endingPage "2074" @default.
• W1965536281 startingPage "2063" @default.
• W1965536281 abstract "The interaction of 6-thioguanine and human serum albumin was investigated by fluorescence, ultraviolet-visible absorption, and surface-enhanced Raman scattering. The fluorescence of human serum albumin decreased with the concentration of 6-thioguanine, and the fluorescence quenching of human serum albumin by 6-thioguanine was static. Molecular modeling showed that 6-thioguanine was located in the hydrophobic cavity in subdomain IIA of human serum albumin. Surface-enhanced Raman scattering was combined with density function theory to characterize the orientation of 6-thioguanine on gold and the 6-thioguanine functional groups bonded to human serum albumin. The 6-thioguanine was shown to be tilted on the gold surface by a N-C˭S moiety. The binding sites of 6-thioguanine to human serum albumin were the NH and amino groups of the pyrimidine ring of 6-thioguanine. This study may provide information regarding the metabolism of anticancer pharmaceuticals in the human body and assist in the development of effective compounds." @default.
• W1965536281 created "2016-06-24" @default.
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• W1965536281 date "2015-04-11" @default.
• W1965536281 modified "2023-10-14" @default.
• W1965536281 title "Characterization of the Interaction of 6-Thioguanine with Human Serum Albumin by Surface-Enhanced Raman Scattering and Molecular Modeling" @default.
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• W1965536281 doi "https://doi.org/10.1080/00032719.2015.1017766" @default.
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