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Exploring binding properties of gliclazide with human serum albumin

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Abstract

The thermodynamic parameters of the binding of gliclazide (GL) with human serum albumin (HSA) have been discussed along with the insight into the nature and mode of the binding. The interaction of GL with HSA was studied using calorimetric technique in combination with UV absorption spectroscopy. UV absorption studies were carried out to ascertain the complex formation between GL and HSA and the calorimetric titrations were performed to determine the stability constant (K = 0.8 × 105 M−1) and enthalpy of binding (∆H = −43.26 kJ mol−1). Van der Waals and hydrogen bonded interaction were found to play a key role in the binding. The mode of binding was ascertained in silico by molecular docking. Calorimetric analysis measure the global change in the property of the system, whereas molecular docking only considers the changes that occurs in the neighboring of the molecule. The magnitude of free enthalpy (∆G) and binding constant calculated from docking studies are in agreement with calorimetrically determined parameters.

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Acknowledgements

The authors are greatly thankful to the University Grants Commission (UGC), New Delhi (F.4-1/2006(BSR)/5-94/2007 dated 03-05-2013) and Council of Scientific and Industrial Research (CSIR), New Delhi (02(0039)/11/EMR-II) for the financial assistance.

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Authors and Affiliations

  1. University Institute of Pharmaceutical Sciences, Panjab University, Chandigarh, 160014, India

    Dimpy Rani, Parnika Goyal & Renu Chadha

  2. Department of Chemistry, Panjab University, Chandigarh, 160014, India

    Dharamvir Singh Jain

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  1. Dimpy Rani
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  2. Parnika Goyal
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  3. Dharamvir Singh Jain
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  4. Renu Chadha
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Correspondence to Renu Chadha.

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Rani, D., Goyal, P., Jain, D.S. et al. Exploring binding properties of gliclazide with human serum albumin. J Therm Anal Calorim 130, 1613–1618 (2017). https://doi.org/10.1007/s10973-017-6416-z

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  • DOI: https://doi.org/10.1007/s10973-017-6416-z

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