Journal
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS
Volume 38, Issue 11, Pages 3178-3187Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/07391102.2019.1652688
Keywords
Human serum albumin (HSA); empagliflozin; dynamic quenching; spectroscopic methods; molecular dynamic simulations; molecular docking
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Funding
- National Natural Science Foundation of China [21808020]
- Applied Basic Research Project of Sichuan Province [2018JY0151]
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Empagliflozin is an oral sodium glucose co-transporter-2 inhibitor for type 2 diabetes mellitus. The interaction between empagliflozin and human serum albumin (HSA) was investigated experimentally and theoretically. Fluorescence quenching and time-resolved fluorescence spectroscopy indicated that the quenching mechanism of empagliflozin and HSA was dynamic and that the effective binding constant at body temperature was 3.495 x 10(3) M-1. Thermodynamic parameters showed that hydrophobic forces were the major binding force in the interaction between empagliflozin and HSA. Circular dichroism, Fourier transform infrared, and 3 D fluorescence spectroscopy revealed that empagliflozin showed a slight change in secondary structure without changing the basic carbon framework of HSA. Site marker displacement experiments revealed that empagliflozin bound to site I of HSA, which was supported by molecular docking. Molecular dynamic simulations indicated that empagliflozin could bind to HSA stably. This study provided insights into the binding mechanism between empagliflozin and HSA. Communicated by Ramaswamy H. Sarma
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