Insights into the effect of glucose on the binding between human serum albumin and the nonsteroidal anti-inflammatory drug nimesulide.

Publication date: Mar 26, 2024

Glucose interacts with human serum albumin (HSA, the main protein responsible for the biodistribution of drugs in the bloodstream) and consequently affects the binding capacity of exogenous compounds. Thus, in this work, the interactive profile between HSA and the anti-inflammatory drug nimesulide (NMD, used mainly by patients with diabetic neuropathy to relieve acute or chronic pains) was characterized in nonglycemic, normoglycemic (80 mg/dL), and hyperglycemic (320 mg/dL) conditions by biophysics techniques. There is a spontaneous and ground-state association HSA:NMD under physiological conditions. Therefore, the Stern-Volmer constant (K) can also be used to estimate the binding affinity. The K values for nonglycemic, normoglycemic, and hyperglycemic conditions are around 10 M, indicating a moderate affinity of NMD to albumin that was slightly improved by glucose levels. Additionally, the binding is enthalpically and entropically driven mainly into subdomains IIA or IIIA. The binding perturbs weakly the α-helix content of albumin, however, glucose potentially stabilizes the tertiary structure, decreasing the structural perturbation upon NMD binding and improves the complex HSA:NMD stability. Overall, the biophysical characterization indicated that glucose levels might slightly positively impact the pharmacokinetic profile of NMD, allowing NMD to achieve its therapeutical potential without affecting drastically its effective dosages.

Concepts Keywords
10m Diabetes mellitus
Biophysics Human serum albumin
Glucose Protein-drug interactions


Type Source Name
drug DRUGBANK Dextrose unspecified form
drug DRUGBANK Human Serum Albumin
disease VO human serum albumin
drug DRUGBANK Nimesulide
disease MESH diabetic neuropathy
disease MESH chronic pains
disease VO effective
disease MESH Diabetes mellitus
disease MESH drug interactions

Original Article

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