Analysis of glipizide binding to normal and glycated human serum albumin by high-performance affinity chromatography.

ABSTRACT: In diabetes, the elevated levels of glucose in the bloodstream can result in the nonenzymatic glycation of proteins such as human serum albumin (HSA). This type of modification has been shown to affect the interactions of some drugs with HSA, including several sulfonylurea drugs that are used to treat type II diabetes. This study used high-performance affinity chromatography (HPAC) to examine the interactions of glipizide (i.e., a second-generation sulfonylurea drug) with normal HSA or HSA that contained various levels of in vitro glycation. Frontal analysis indicated that glipizide was interacting with both normal and glycated HSA through two general groups of sites: a set of relatively strong interactions and a set of weaker interactions with average association equilibrium constants at

SUBMITTER: Matsuda R 

PROVIDER: S-EPMC6359935 | biostudies-literature | 2015 Jul

REPOSITORIES: biostudies-literature