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Vol. 32 No. 7 (2020): Vol 32 Issue 7

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Interaction Between α-Glucosidase Inhibitor with Common Blood Proteins: A Thermodynamic and Spectroscopic Studies

K.M. Sachin
School of Chemical Sciences, Central University of Gujarat, Sector-30, Gandhinagar-382030, India
https://orcid.org/0000-0003-3766-2588
Sameer A. Karpe
School of Chemical Sciences, Central University of Gujarat, Sector-30, Gandhinagar-382030, India
https://orcid.org/0000-0002-4012-584X
Man Singh
School of Chemical Sciences, Central University of Gujarat, Sector-30, Gandhinagar-382030, India
https://orcid.org/0000-0002-0706-3763
Ajaya Bhattarai
Department of Chemistry, M.M.A.M. Campus, Tribhuvan University, Biratnagar, Nepal
https://orcid.org/0000-0002-2648-4686

Corresponding Author(s) : Ajaya Bhattarai

bkajaya@yahoo.com

Asian Journal of Chemistry, Vol. 32 No. 7 (2020): Vol 32 Issue 7

Abstract

The interaction of an α-glucosidase inhibitors class of drug acarbose with globular proteins like bovine serum albumin (BSA), human serum albumin (HSA) and haemoglobin studied by fluorescence, circular dichroism (CD) spectroscopic methods. Acarbose is used for the treatment of diabetes mellitus type 2 and in some countries, prediabetes. The quenching constant (kq) values were calculated by using fluorescence data, higher with haemoglobin (at λext = 405 nm). It indicates the quenching process for the acarbose-haemoglobin interaction. Thus, the binding constants (kb), infers that the electrostatic, hydrogen bonding, and intermolecular interactions play an important role in the proteins, and drug interaction. The number of binding sites (n), between BSA, HSA and haemoglobin with acarbose was estimated by fluorescence data, the highest binding sites (15.55) of acarbose-haemoglobin at (λext = 405 nm) indicates that the strong interaction or high quenching interaction. The interactions between BSA, HSA and haemoglobin with acarbose were confirmed by spectroscopic analysis and thermodynamic determination. The circular dichroism (CD) spectra implied the significant change in the conformation of BSA, HSA and haemoglobin upon binding with acarbose.

Keywords

Globular proteins α-Glucosidase Quenching constant Binding constant Gibbs free Energy Circular dichroism
Sachin, K., Karpe, S. A., Singh, M., & Bhattarai, A. (2020). Interaction Between α-Glucosidase Inhibitor with Common Blood Proteins: A Thermodynamic and Spectroscopic Studies. Asian Journal of Chemistry, 32(7), 1756–1762. Retrieved from https://asianpubs.org/index.php/ajchem/article/view/2402
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