Download Albumin in Medicine: Pathological and Clinical Applications by Masaki Otagiri, Victor Tuan Giam Chuang PDF

By Masaki Otagiri, Victor Tuan Giam Chuang

This ebook offers a finished assessment of scientific and pharmaceutical purposes of human serum albumin (HSA), with updates on structural facets of albumin from the views of X-ray crystallography and NMR, endogenous and exogenous ligand binding of albumin in numerous pathological stipulations, and genetic editions and their phenotypes. speedy development and improvement of its functions have led to extraordinary effects for which albumin has in actual fact been confirmed to be a powerful biomaterial. Contributions from major overseas specialists during this box exhibit how HSA is utilized to analysis, remedy, medicines, and therapy, with a finished advent of HSA. This quantity will attract scientists in pharmaceutical and scientific study together with pharmaceutical chemists, pharmacokineticists, toxicologists, and biochemists not just in academia but in addition in undefined. Readers can successfully collect the newest wisdom of purposes of HSA and its influence on human future health in one volume.

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Example text

2006) HSA-hGH (Osborn et al. 2002) Form Lyophilized Powder Brand name Abraxane® Use Metastatic breast cancer Characteristics HSA-bound Paclitaxel (nanoparticle) Active Nab-Paclitaxel (Hawkins et al. 4 Example of pharmaceutical products containing HSA as DDS carrier Vial Vial – Vial Vial Vial Prefilled Syringe Container Grass vial Phase I Phase II/III (enrolled) Phase III (submitted BLA) Phase I Phase III (withdrawn BLA, MAA) Phase II Phase III (withdrawn BLA) Marketed Status Marketed – – Effects of surfactant and substitution of 34 Cys (Zhao et al.

They suggested that surfactants be employed as a rational approach to stabilizing protein pharmaceuticals such as Albutropin™. Recently, Cordes et al. investigated the effect of selective HSA domain stabilization by octanoic acid on the aggregation of HSA-hGH (Cordes et al. 2012b). They demonstrated that the reduction of aggregation under solution conditions is due to an increased colloidal stability resulting from the binding of octanoate to the HSA domain, but not due to an increased conformational stability of the HSA domain.

1998). Increasing the temperature to about 50 °C results in the reversible separation of domains I and II, as evidenced by fluorescent techniques. They also reported that heating to < 70 °C resulted in the irreversible unfolding of domain II, while increasing the temperature to 70 °C or higher resulted in the irreversible unfolding of domain I. It was suggested that this irreversible unfolding is accompanied by the unfolding of the pocket containing the free sulfhydryl group of 34Cys, which enables the formation of aggregates through disulfide bridges.

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