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dc.contributor.authorTaguchi, K.
dc.contributor.authorChuang, Victor
dc.contributor.authorYamasaki, K.
dc.contributor.authorOtagiri, M.
dc.identifier.citationTaguchi, K. and Chuang, V. and Yamasaki, K. and Otagiri, M. 2015. Pharmacokinetically modified human serum albumin based therapeutic design and development, in Stokes, T. (ed), Human Serum Albumin (HSA): Functional Structure, Synthesis and Therapeutic Uses, pp. 69-89. New York: Nova Publishers.

Human serum albumin (HSA) is synthesized predominantly in the liver, and has an extraordinarily long circulatory half-life (~19 days). Since HSA is responsible for 80% of the colloidal osmotic pressure of plasma, the patients with hypoalbuminemia are typically given a plasma expander to increase the plasma volume. Clinically, using HSA as an extender is preferable to other options, such as dextran, hydroxylethyl starch, due to its long retention in plasma. However, the circulatory half-life of HSA is significantly- impacted by structural changes of HSA and pathological conditions. Recent scientific advances have revealed new information regarding the factors that influence the pharmacokinetic properties of HSA. In this chapter, we provide an overview of the impact of HSA structure and biotransformation upon the pharmacokinetic properties of HSA, and discuss new possibilities for the therapeutic potential of HSA based on its pharmacokinetic properties.

dc.titlePharmacokinetically modified human serum albumin based therapeutic design and development
dc.typeBook Chapter
dcterms.source.titleHuman Serum Albumin (HSA): Functional Structure, Synthesis and Therapeutic Uses
curtin.departmentSchool of Pharmacy
curtin.accessStatusFulltext not available

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