Studies of drug interactions with glycated human serum albumin by high-performance affinity chromatography
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 c...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
| Published: |
De Gruyter
2014-08-01
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| Series: | Reviews in Analytical Chemistry |
| Subjects: | |
| Online Access: | https://doi.org/10.1515/revac-2013-0029 |
| _version_ | 1819115374846672896 |
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| author | Matsuda Ryan Kye So-Hwang Anguizola Jeanethe Hage David S. |
| author_facet | Matsuda Ryan Kye So-Hwang Anguizola Jeanethe Hage David S. |
| author_sort | Matsuda Ryan |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-22T05:00:11Z |
| format | Article |
| id | doaj.art-878a2fa384c3462891f6369108020f8e |
| institution | Directory Open Access Journal |
| issn | 0793-0135 2191-0189 |
| language | English |
| last_indexed | 2024-12-22T05:00:11Z |
| publishDate | 2014-08-01 |
| publisher | De Gruyter |
| record_format | Article |
| series | Reviews in Analytical Chemistry |
| spelling | doaj.art-878a2fa384c3462891f6369108020f8e2022-12-21T18:38:17ZengDe GruyterReviews in Analytical Chemistry0793-01352191-01892014-08-01332799410.1515/revac-2013-0029Studies of drug interactions with glycated human serum albumin by high-performance affinity chromatographyMatsuda Ryan0Kye So-Hwang1Anguizola Jeanethe2Hage David S.3Department of Chemistry, University of Nebraska, Lincoln, NE 68588-0304, USADepartment of Chemistry, University of Nebraska, Lincoln, NE 68588-0304, USADepartment of Chemistry, University of Nebraska, Lincoln, NE 68588-0304, USADepartment of Chemistry, University of Nebraska, Lincoln, NE 68588-0304, USADiabetes 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.https://doi.org/10.1515/revac-2013-0029binding studiesdiabetesdrug-protein bindinghuman serum albuminglycationhigh-performance affinity chromatographysulfonylurea drugs |
| spellingShingle | Matsuda Ryan Kye So-Hwang Anguizola Jeanethe Hage David S. Studies of drug interactions with glycated human serum albumin by high-performance affinity chromatography Reviews in Analytical Chemistry binding studies diabetes drug-protein binding human serum albumin glycation high-performance affinity chromatography sulfonylurea drugs |
| title | Studies of drug interactions with glycated human serum albumin by high-performance affinity chromatography |
| title_full | Studies of drug interactions with glycated human serum albumin by high-performance affinity chromatography |
| title_fullStr | Studies of drug interactions with glycated human serum albumin by high-performance affinity chromatography |
| title_full_unstemmed | Studies of drug interactions with glycated human serum albumin by high-performance affinity chromatography |
| title_short | Studies of drug interactions with glycated human serum albumin by high-performance affinity chromatography |
| title_sort | studies of drug interactions with glycated human serum albumin by high performance affinity chromatography |
| topic | binding studies diabetes drug-protein binding human serum albumin glycation high-performance affinity chromatography sulfonylurea drugs |
| url | https://doi.org/10.1515/revac-2013-0029 |
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