High-Performance affinity chromatographic studies of repaglinide and nateglinide interactions with normal and glyoxal- or methylglyoxal-modified human albumin serum.

ABSTRACT: During diabetes human serum albumin (HSA), an important drug transport protein, can be modified by agents such as glyoxal (Go) and methylglyoxal (MGo) to form advanced glycation end-products. High-performance affinity microcolumns and zonal elution competition studies were used to compare interactions by the anti-diabetic drugs repaglinide and nateglinide with normal and Go- or MGo-modified HSA at Sudlow sites I and II of this protein. Both drugs had their strongest binding at Sudlow site II for the normal and modified forms of HSA. The association equilibrium constants at this site for repaglinide and nateglinide with normal HSA were 6.1 (± 0.2) × 10⁴ M^-1 and 7.1 (± 0.8) × 10⁵ M^-1, respectively, at pH 7.4 and 37⁰C; these values increased by up t

SUBMITTER: Ovbude ST 

PROVIDER: S-EPMC8169628 | biostudies-literature | 2021 Jul

REPOSITORIES: biostudies-literature