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Interaction between Human Serum Albumin and antidiabetic compounds and its influence on the O2(1Δg)-mediated degradation of the protein

Paper ID Volume ID Publish Year Pages File Format Full-Text
29778 44440 2015 9 PDF Available
Title
Interaction between Human Serum Albumin and antidiabetic compounds and its influence on the O2(1Δg)-mediated degradation of the protein
Abstract

•Fluorescence and docking assays showed that Gli and Glip bind to HSA on two sites.•The interaction between HSA and Glip is a favored, enthalpically-controlled process.•Glip is less photooxidizable than Gli through a O2(1Δg)-mediated process.•The HSA–Andb binding cause a decrease in the overall rate constant for O2(1Δg) quenching.

The complexity depicted by disease scenarios as diabetes mellitus, constitutes a very interesting field of study when drugs and biologically relevant components may be affected by such environments. In this report, the interaction between the protein Human Serum Albumin (HSA) and two antidiabetics (Andb), Gliclazide (Gli) and Glipizide (Glip) was studied through fluorescence and docking assays, in order to characterize these systems. On the basis that HSA and Andb can be exposed in vivo at high Reactive Oxygen Species (ROS) concentrations in diabetic patients, the degradative process of the protein free and bound to Andb, in presence of the species singlet molecular oxygen (O2(1Δg)), was evaluated. Fluorescence and docking assays indicated that Gli, as well as Glip bind to HSA on two sites, with binding constants values in the order of 104–105 M−1. Likewise, docking assays revealed that the location of Gli or Glip on the protein may be the HSA binding sites II and III. Thermodynamic parameters showed that the interaction between HSA and Glip is a favored, enthalpically-controlled process. Oxygen uptake experiments indicated that Glip is less photooxidizable than Gli through a O2(1Δg)-mediated process. Besides, the protein–Andb binding produced a decrease in the overall rate constant for O2(1Δg) quenching as compared to the value for the free protein. This fact could be interpreted in terms of a reduction in the availability of Tyrosine residues in the bonded protein, with a concomitant decrease in the physical quenching deactivation of the oxidative species.

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Interaction between Human Serum Albumin and antidiabetic compounds and its influence on the O2(1Δg)-mediated degradation of the protein
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology B: Biology - Volume 142, January 2015, Pages 20–28
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us