Literature DB >> 26526139

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

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

Abstract

Diabetes is a health condition associated with 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 blood to the transport protein human serum albumin (HSA). One consequence of the elevated levels of glucose in diabetes is the non-enzymatic 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.

Entities:  

Keywords:  binding studies; diabetes; drug-protein binding; glycation; high-performance affinity chromatography; human serum albumin; sulfonylurea drugs

Year:  2014        PMID: 26526139      PMCID: PMC4623599          DOI: 10.1515/revac-2013-0029

Source DB:  PubMed          Journal:  Rev Anal Chem        ISSN: 0793-0135            Impact factor:   3.067


  48 in total

1.  Biosensor alternative: frontal affinity chromatography.

Authors:  David C Schriemer
Journal:  Anal Chem       Date:  2004-12-01       Impact factor: 6.986

2.  Studies by biointeraction chromatography of binding by phenytoin metabolites to human serum albumin.

Authors:  Corey M Ohnmacht; Shirley Chen; Zenghan Tong; David S Hage
Journal:  J Chromatogr B Analyt Technol Biomed Life Sci       Date:  2006-04-18       Impact factor: 3.205

3.  Effects of ligand heterogeneity in the characterization of affinity columns by frontal analysis.

Authors:  S A Tweed; B Loun; D S Hage
Journal:  Anal Chem       Date:  1997-12-01       Impact factor: 6.986

4.  Quantitative analysis of glycation patterns in human serum albumin using 16O/18O-labeling and MALDI-TOF MS.

Authors:  Omar S Barnaby; Ronald L Cerny; William Clarke; David S Hage
Journal:  Clin Chim Acta       Date:  2011-05-13       Impact factor: 3.786

5.  Locating high-affinity fatty acid-binding sites on albumin by x-ray crystallography and NMR spectroscopy.

Authors:  J R Simard; P A Zunszain; C-E Ha; J S Yang; N V Bhagavan; I Petitpas; S Curry; J A Hamilton
Journal:  Proc Natl Acad Sci U S A       Date:  2005-12-05       Impact factor: 11.205

Review 6.  In silico prediction of drug-binding strengths to human serum albumin.

Authors:  Gonzalo Colmenarejo
Journal:  Med Res Rev       Date:  2003-05       Impact factor: 12.944

7.  Analysis of drug interactions with modified proteins by high-performance affinity chromatography: binding of glibenclamide to normal and glycated human serum albumin.

Authors:  Ryan Matsuda; Jeanethe Anguizola; K S Joseph; David S Hage
Journal:  J Chromatogr A       Date:  2012-10-08       Impact factor: 4.759

8.  Localization of tolbutamide binding sites on human serum albumin using titration calorimetry and heteronuclear 2-D NMR.

Authors:  M G Jakoby; D F Covey; D P Cistola
Journal:  Biochemistry       Date:  1995-07-11       Impact factor: 3.162

9.  Allosteric and competitive displacement of drugs from human serum albumin by octanoic acid, as revealed by high-performance liquid affinity chromatography, on a human serum albumin-based stationary phase.

Authors:  T A Noctor; I W Wainer; D S Hage
Journal:  J Chromatogr       Date:  1992-06-10

10.  Nonenzymatic glycosylation of albumin in vivo. Identification of multiple glycosylated sites.

Authors:  N Iberg; R Flückiger
Journal:  J Biol Chem       Date:  1986-10-15       Impact factor: 5.157

View more
  3 in total

1.  Analysis of multi-site drug-protein interactions by high-performance affinity chromatography: Binding by glimepiride to normal or glycated human serum albumin.

Authors:  Ryan Matsuda; Zhao Li; Xiwei Zheng; David S Hage
Journal:  J Chromatogr A       Date:  2015-07-06       Impact factor: 4.759

2.  Binding studies based on ultrafast affinity extraction and single- or two-column systems: Interactions of second- and third-generation sulfonylurea drugs with normal or glycated human serum albumin.

Authors:  Bao Yang; Xiwei Zheng; David S Hage
Journal:  J Chromatogr B Analyt Technol Biomed Life Sci       Date:  2018-10-17       Impact factor: 3.205

3.  Studies of binding by sulfonylureas with glyoxal- and methylglyoxal-modified albumin by immunoextraction using affinity microcolumns.

Authors:  Elliott L Rodriguez; Pingyang Tao; Ashley G Woolfork; Zhao Li; Ryan Matsuda; Zuchen Sun; David S Hage
Journal:  J Chromatogr A       Date:  2020-11-10       Impact factor: 4.759

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.