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- W2019968556 abstract "In the present study, the interactions of urocanic acid (UA) with bovine serum albumins (BSA) at pH 5.0 and 7.4 were investigated by means of docking simulations. The binding modes of trans- and cis-UA to BSA at pH 5.0 and 7.4 were analysed. In addition, the theoretically predicted binding abilities of zwitterion and anion of UA with BSA are in good agreement with the experimental results. Through comparison with the binding patterns, we revealed that the stronger interactions of UA anion with BSA relative to the zwitterion primarily result from: (1) the increased number of hydrogen bonds between UA anion and BSA; (2) the attractive electrostatic interaction between the deprotoned carboxyl group in UA anion and Arg433 in comparison with the repulsion between the imidazole moiety in zwitterion and the same residue in BSA. This provides a rational explanation for the experimental finding that the binding of UA to BSA at pH 7.4 is much stronger than at pH 5.0." @default.
- W2019968556 created "2016-06-24" @default.
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- W2019968556 date "2010-01-01" @default.
- W2019968556 modified "2023-09-24" @default.
- W2019968556 title "Interactions of urocanic acid with bovine serum albumin and the influence of pH on binding affinities: a docking simulation study" @default.
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- W2019968556 doi "https://doi.org/10.1080/08927020903108091" @default.
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