Chromatographic studies of changes in binding of sulfonylurea drugs to human serum albumin due to glycation and fatty acids.
Article Details
- CitationCopy to clipboard
Basiaga SB, Hage DS
Chromatographic studies of changes in binding of sulfonylurea drugs to human serum albumin due to glycation and fatty acids.
J Chromatogr B Analyt Technol Biomed Life Sci. 2010 Nov 15;878(30):3193-7. doi: 10.1016/j.jchromb.2010.09.033. Epub 2010 Oct 23.
- PubMed ID
- 20974553 [ View in PubMed]
- Abstract
This report examines the use of high-performance affinity chromatography as a screening tool for studying the change in binding by sulfonylurea drugs to the protein human serum albumin (HSA) during diabetes. The effects of both the non-enzymatic glycation of HSA and the presence of fatty acids on these interactions were considered using a zonal elution format. It was found that there was a significant increase (i.e., 2.7- to 3.6-fold) in the relative retention of several sulfonylurea drugs (i.e., acetohexamide, tolbutamide, glybenclamide and gliclazide) on columns containing normal versus glycated HSA. The addition of various long chain fatty acids to the mobile phase gave the same trend in retention for the tested drugs on both the HSA and glycated HSA columns, generally leading to lower binding. Most of the fatty acids examined produced similar or moderately different relative shifts in retention; however, palmitic acid was found to produce a much larger change in retention on columns containing glycated HSA versus normal HSA under the conditions used in this study.
DrugBank Data that Cites this Article
- Drug Carriers
Drug Carrier Kind Organism Pharmacological Action Actions Acetohexamide Serum albumin Protein Humans UnknownNot Available Details Tolbutamide Serum albumin Protein Humans UnknownNot Available Details