Details

Autor(en) / Beteiligte

• Rahman, Safikur
• Rehman, Md Tabish
• Rabbani, Gulam
• Khan, Parvez
• AlAjmi, Mohamed F
• Hassan, Md Imtaiyaz
• Muteeb, Ghazala
• Kim, Jihoe

Titel

Insight of the Interaction between 2,4-thiazolidinedione and Human Serum Albumin: A Spectroscopic, Thermodynamic and Molecular Docking Study

Ist Teil von

• International journal of molecular sciences, 2019-06, Vol.20 (11), p.2727

Ort / Verlag

Switzerland: MDPI AG

Erscheinungsjahr

2019

Quelle

EZB Free E-Journals

Beschreibungen/Notizen

• Thiazolidinedione derivatives (TZDs) have attracted attention because of their pharmacological effects. For example, certain TZDs have been reported to ameliorate type II diabetes by binding and activating PPARs (peroxisome proliferator-activated receptors). Nonetheless, no information is available on the interaction between the heterocyclic 2, 4-thiazolidinedione (2,4-TZD) moiety and serum albumin, which could affect the pharmacokinetics and pharmacodynamics of TZDs. In this study, we investigated the binding of 2,4-TZD to human serum albumin (HSA). Intrinsic fluorescence spectroscopy revealed a 1:1 binding stoichiometry between 2,4-TZD and HSA with a binding constant ( ) of 1.69 ± 0.15 × 10 M at 298 K. Isothermal titration calorimetry studies showed that 2,4-TZD/HSA binding was an exothermic and spontaneous reaction. Molecular docking analysis revealed that 2,4-TZD binds to HSA subdomain IB and that the complex formed is stabilized by van der Waal's interactions and hydrogen bonds. Molecular dynamics simulation confirmed the stability of the HSA-TZD complex. Further, circular dichroism and 3D fluorescence studies showed that the global conformation of HSA was slightly altered by 2,4-TZD binding, enhancing its stability. The results obtained herein further help in understanding the pharmacokinetic properties of thiazolidinedione.