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• W2548898110 endingPage "192" @default.
• W2548898110 startingPage "187" @default.
• W2548898110 abstract "Lamotrigine (an epileptic drug) interaction with human serum albumin (HSA) was investigated by fluorescence, UV–Vis, FTIR, CD spectroscopic techniques, and molecular modeling methods. Binding constant (Kb) of 5.74 × 103 and number of binding site of 0.97 showed that there is a slight interaction between lamotrigine and HSA. Thermodynamic studies was constructed using the flourimetric titrations in three different temperatures and the resulted data used to calculate the parameters using Vant Hoff equation. Decreased Stern Volmer quenching constant by enhanced temperature revealed the static quenching mechanism. Negative standard enthalpy (ΔH) and standard entropy (ΔS) changes indicated that van der Waals interactions and hydrogen bonds were dominant forces which facilitate the binding of Lamotrigine to HSA, the results were confirmed by molecular docking studies which showed no hydrogen binding. The FRET studies showed that there is a possibility of energy transfer between Trp214 and lamotrigine. Also the binding of lamotrigine to HSA in the studied concentrations was not as much as many other drugs, but the secondary structure of the HSA was significantly changed following the interaction in a way that α-helix percentage was reduced from 67% to 57% after the addition of lamotrigine in the molar ratio of 4:1 to HSA. According to the docking studies, lamotrigine binds to IB site preferably." @default.
• W2548898110 created "2016-11-11" @default.
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• W2548898110 date "2017-01-01" @default.
• W2548898110 modified "2023-10-12" @default.
• W2548898110 title "Interaction of an antiepileptic drug, lamotrigine with human serum albumin (HSA): Application of spectroscopic techniques and molecular modeling methods" @default.
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• W2548898110 doi "https://doi.org/10.1016/j.jphotobiol.2016.09.046" @default.
• W2548898110 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27951518" @default.
• W2548898110 hasPublicationYear "2017" @default.
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