Abstract
Human serum albumin (HSA) is the most abundant protein in the plasma. HSA plays a central role in drug pharmacokinetics because most drugs bound to HSA are delivered to their target organ/tissues. The prodrug strategies have shown great promise for improving the activity and selectivity of drugs. Designing prodrugs based on special HSA residues, such as Cys34 and Lys residues, has been extensively studied. Therefore, this review provides an overview of the development of nonsteroidal anti-inflammatory and anticancer prodrugs based on these special residues. In conclusion, this review may guide the rational design and development of new prodrugs for future clinical applications.
Keywords: Human serum albumin, Prodrug, Drug design, Protein structure.
Graphical Abstract
Current Topics in Medicinal Chemistry
Title:Designing Prodrugs Based on Special Residues of Human Serum Albumin
Volume: 16 Issue: 9
Author(s): Yi Gou, Feng Yang and Hong Liang
Affiliation:
Keywords: Human serum albumin, Prodrug, Drug design, Protein structure.
Abstract: Human serum albumin (HSA) is the most abundant protein in the plasma. HSA plays a central role in drug pharmacokinetics because most drugs bound to HSA are delivered to their target organ/tissues. The prodrug strategies have shown great promise for improving the activity and selectivity of drugs. Designing prodrugs based on special HSA residues, such as Cys34 and Lys residues, has been extensively studied. Therefore, this review provides an overview of the development of nonsteroidal anti-inflammatory and anticancer prodrugs based on these special residues. In conclusion, this review may guide the rational design and development of new prodrugs for future clinical applications.
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Cite this article as:
Gou Yi, Yang Feng and Liang Hong, Designing Prodrugs Based on Special Residues of Human Serum Albumin, Current Topics in Medicinal Chemistry 2016; 16 (9) . https://dx.doi.org/10.2174/1568026615666150825142908
DOI https://dx.doi.org/10.2174/1568026615666150825142908 |
Print ISSN 1568-0266 |
Publisher Name Bentham Science Publisher |
Online ISSN 1873-4294 |
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