Version 1
: Received: 4 August 2024 / Approved: 5 August 2024 / Online: 5 August 2024 (08:19:14 CEST)
How to cite:
Szkudlarek, A. Spectroscopic Investigation of Losartan and Glipizide Competitive Binding to Glycated Albumin in Polypharmacotherapy: A Comparative Study. Preprints2024, 2024080250. https://doi.org/10.20944/preprints202408.0250.v1
Szkudlarek, A. Spectroscopic Investigation of Losartan and Glipizide Competitive Binding to Glycated Albumin in Polypharmacotherapy: A Comparative Study. Preprints 2024, 2024080250. https://doi.org/10.20944/preprints202408.0250.v1
Szkudlarek, A. Spectroscopic Investigation of Losartan and Glipizide Competitive Binding to Glycated Albumin in Polypharmacotherapy: A Comparative Study. Preprints2024, 2024080250. https://doi.org/10.20944/preprints202408.0250.v1
APA Style
Szkudlarek, A. (2024). Spectroscopic Investigation of Losartan and Glipizide Competitive Binding to Glycated Albumin in Polypharmacotherapy: A Comparative Study. Preprints. https://doi.org/10.20944/preprints202408.0250.v1
Chicago/Turabian Style
Szkudlarek, A. 2024 "Spectroscopic Investigation of Losartan and Glipizide Competitive Binding to Glycated Albumin in Polypharmacotherapy: A Comparative Study" Preprints. https://doi.org/10.20944/preprints202408.0250.v1
Abstract
Understanding the interaction between pharmaceuticals and serum proteins is crucial for optimizing therapeutic strategies, especially in patients with coexisting chronic diseases. The primary goal of this study was to assess the potential changes in binding affinity and competition between glipizide (GLP, a second-generation sulfonylurea hypoglycemic drug) and losartan (LOS, a medication commonly prescribed for hypertension, particularly for patients with concurrent diabetes) with non-glycated (HSA) and glycated (gHSAGLC, gHSAFRC) human serum albumin using multiple spectroscopic techniques (fluorescence, UV-visible absorption, and circular dichroism spectroscopy). The results indicate that FRC is a more effective glycation agent for HSA than GLC, significantly altering the albumin structure and affecting the microenvironment around critical amino acid residues, Trp-214 and Tyr. These modifications reduce the binding affinity of LOS and GLP to gHSAGLC and gHSAFRC, compared to HSA, resulting in less stable drug-protein complexes. The study reveals that LOS and GLP interact nonspecifically with the hydrophobic regions of the albumin surface in both binary (ligand-albumin) and ternary systems (ligand-albumin-ligandconst) and specifically saturate the binding sites within the protein molecule. Furthermore, the presence of an additional drug (GLP in the LOS-albumin complex or LOS in the GLP-albumin complex) complicates the interactions, likely leading to competitive binding or displacement of the initially bound drug in both non-glycated and glycated albumins. Analysis of the CD spectra suggests mutual interactions between GLP and LOS, underscoring the importance of closely monitoring patients co-administered these drugs to ensure optimal therapeutic efficacy and safety. Początek formularzaDół formularza
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
