Binding of sulfonylurea derivatives to bovine serum albumin: part I. Binding of SPC--703, tolbutamide, glibornuride and glipizide

Wójcikowski, C.; Szlabowicz, D.

Polish Journal of Pharmacology and Pharmacy 29(5): 469-475

1977


ISSN/ISBN: 0301-0244
PMID: 22846
Accession: 068518283

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Abstract
Four labeled sulfonyled sulfonylureas, 14C-SPC-703 = 6.8 .cntdot. 103 M-1), tolbutamide (k1 = 19.3 .times. 103 M-1) and glipizide (k1 = 12.4 .times. 103 M-1), and up to 5 molecules of glibornuride (k1 = 5.2 .times. 103 M-1). (The low-affinity sites can bind 8.8 and 12 molecules of the sulfonylureas, respectively (k2 = 1.2-1.3 .times. 103 M-1).) The affinity of sulfonylureas to BSA increases with protein concentration, temperature and pH. Other sulfonylurea derivatives decreased the binding of tested drugs to BSA in a competitive manner. The inhibition of binding was the lowest for glibornuride. Sulfonylureas most probably bind to albumin at common sites. The bonds may have a hydrophobic character.