Protective ability and binding affinity of captopril towards serum albumin in an in vitro glycation model of diabetes mellitus.

Article Details

Citation

Copy to clipboard

Mariee AD, Al-Shabanah O

Protective ability and binding affinity of captopril towards serum albumin in an in vitro glycation model of diabetes mellitus.

J Pharm Biomed Anal. 2006 May 3;41(2):571-5. Epub 2006 Feb 15.

PubMed ID

16469467 [ View in PubMed

]

Abstract

One-quarter of adult population in different world regions are reported to live with hypertension, of whom, a high percentage had a diabetes mellitus (DM). This co-morbid state is believed to act synergistically on accelerating the long-term diabetic complications. Therefore, adequate treatment of high blood pressure is essential for diabetic patients, and should be always directed to their benefits. Albumin glycation is still the most important explanation for the pathogenesis of chronic diabetic complications. Our in vitro experiments induce non-enzymatic glycation of bovine serum albumin (BSA) under physiological conditions. The levels of advanced glycation end products (AGEs) were measured by their characteristic intrinsic fluorescence. Additions of captopril at concentrations from 5 to 50 microM caused 10-47% reduction in the formation of AGEs. Captopril binding properties of native and glycosylated BSA were characterized, and its affinity towards the native albumin was unaltered by the in vitro glycation. Therefore, we concluded that captopril could protect against albumin glycation, and it has a similar binding affinities towards native and glcosylated protein. Anti-glycation effect may help to attenuate the serious long-term diabetes related complications. Besides, the unchanged pharmacokinetic parameters provide an essential extra beneficial effect for diabetic hypertensive patients.

DrugBank Data that Cites this Article

Drug Carriers

Drug	Carrier	Kind	Organism	Pharmacological Action	Actions
Captopril	Serum albumin	Protein	Humans	No	Other/unknown	Details