Abstract
Human serum albumin (HSA) regulates the transport and availability of numerous chemical compounds and molecules in the blood vascular system. While previous HSA research has found that HSA interacts with specific varieties of ligands, new research efforts aim to expand HSA’s ability to interact with more different drugs in order to improve the delivery of various pharmacological drugs. This review will cover fatty acid chain and posttranslational modifications of HSA that potentially modulate how HSA interacts with various pharmacological drugs, including glycation, cysteinylation, S-nitrosylation, S-transnitrosation and S-guanylation.
Keywords: Human serum albumin.
Current Pharmaceutical Design
Title:Review: Modifications of Human Serum Albumin and their Binding Effect
Volume: 21 Issue: 14
Author(s): Philbert Lee and Xiaoyang Wu
Affiliation:
Keywords: Human serum albumin.
Abstract: Human serum albumin (HSA) regulates the transport and availability of numerous chemical compounds and molecules in the blood vascular system. While previous HSA research has found that HSA interacts with specific varieties of ligands, new research efforts aim to expand HSA’s ability to interact with more different drugs in order to improve the delivery of various pharmacological drugs. This review will cover fatty acid chain and posttranslational modifications of HSA that potentially modulate how HSA interacts with various pharmacological drugs, including glycation, cysteinylation, S-nitrosylation, S-transnitrosation and S-guanylation.
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Cite this article as:
Lee Philbert and Wu Xiaoyang, Review: Modifications of Human Serum Albumin and their Binding Effect, Current Pharmaceutical Design 2015; 21 (14) . https://dx.doi.org/10.2174/1381612821666150302115025
DOI https://dx.doi.org/10.2174/1381612821666150302115025 |
Print ISSN 1381-6128 |
Publisher Name Bentham Science Publisher |
Online ISSN 1873-4286 |
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