Studies of drug interactions with glycated human serum albumin by high-performance affinity chromatography

Ryan Matsuda, So Hwang Kye, Jeanethe Anguizola, David S. Hage

Research output: Contribution to journalArticle

9 Scopus citations

Abstract

Diabetes is a health condition associated with the elevated levels of glucose in the bloodstream and affects 366 million people worldwide. Type II diabetes is often treated with sulfonylurea drugs, which are known to bind tightly in the blood to the transport protein human serum albumin (HSA). One consequence of the elevated levels of glucose in diabetes is the nonenzymatic glycation of proteins such as HSA. Several areas of HSA are now known to be affected by glycation-related modifications, which may in turn affect the binding of sulfonylurea drugs and other solutes to this protein. This review discusses some recent studies that have examined these changes in drug-protein binding by employing high-performance affinity chromatography (HPAC). A description of the theoretical and experimental techniques that were used in these studies is given. The information on drug interactions with glycated HSA, as obtained through this method, is also summarized. In addition, the potential advantages of this approach in the areas of biointeraction analysis and personalized medicine are considered.

Original languageEnglish (US)
Pages (from-to)79-94
Number of pages16
JournalReviews in Analytical Chemistry
Volume33
Issue number2
DOIs
StatePublished - Aug 1 2014

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Keywords

  • Binding studies
  • Diabetes
  • Drug-protein binding
  • Glycation
  • High-performance affinity chromatography
  • Human serum albumin
  • Sulfonylurea drugs

ASJC Scopus subject areas

  • Analytical Chemistry

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