Litcius/Paper detail

How Does Glycation Affect Binding Parameters of the Albumin-Gliclazide System in the Presence of Drugs Commonly Used in Diabetes? In Vitro Spectroscopic Study

Katarzyna Wiglusz, Ewa Żurawska-Płaksej, Anna Rorbach-Dolata, Agnieszka Piwowar

2021Molecules13 citationsDOIOpen Access PDF

Abstract

In this research, the selected drugs commonly used in diabetes and its comorbidities (gliclazide, cilazapril, atorvastatin, and acetylsalicylic acid) were studied for their interactions with bovine serum albumin—native and glycated. Two different spectroscopic methods, fluorescence quenching and circular dichroism, were utilized to elucidate the binding interactions of the investigational drugs. The glycation process was induced in BSA by glucose and was confirmed by the presence of advanced glycosylation end products (AGEs). The interaction between albumin and gliclazide, with the presence of another drug, was confirmed by calculation of association constants (0.11–1.07 × 104 M−1). The nature of changes in the secondary structure of a protein depends on the drug used and the degree of glycation. Therefore, these interactions may have an influence on pharmacokinetic parameters.

Topics & Concepts

GlycationGliclazideChemistryBovine serum albuminCircular dichroismPharmacologyDiabetes mellitusDrugAlbuminGlycosylationBinding constantPlasma protein bindingBiochemistryBinding siteMedicineEndocrinologyReceptorProtein Interaction Studies and Fluorescence AnalysisDrug Transport and Resistance MechanismsSurfactants and Colloidal Systems