Characterization of binding by sulfonylureas with normal or modified human serum albumin using affinity microcolumns prepared by entrapment.

ABSTRACT: Modification of proteins can occur during diabetes due to the formation of advanced glycation end-products (AGEs) with reactive dicarbonyls such as glyoxal (Go) and methylglyoxal (MGo). Human serum albumin (HSA) is a serum protein that binds to many drugs in blood and that is known to be modified by Go and MGo. This study examined the binding of various sulfonylurea drugs with these modified forms of HSA by using high-performance affinity microcolumns prepared by non-covalent protein entrapment. Zonal elution experiments were employed to compare the retention and overall binding constants for the drugs with Go- or MGo-modified HSA vs normal HSA. The results were compared to values from the literature, such as measured or estimated using affinity columns containing covalently immobilized HS

SUBMITTER: Poddar S 

PROVIDER: S-EPMC10529298 | biostudies-literature | 2023 Jul

REPOSITORIES: biostudies-literature