By Masaki Otagiri, Victor Tuan Giam Chuang
This e-book provides a accomplished assessment of scientific and pharmaceutical functions of human serum albumin (HSA), with updates on structural features of albumin from the views of X-ray crystallography and NMR, endogenous and exogenous ligand binding of albumin in a variety of pathological stipulations, and genetic versions and their phenotypes. speedy development and improvement of its functions have ended in amazing effects for which albumin has sincerely been confirmed to be a strong biomaterial. Contributions from top overseas specialists during this box convey how HSA is utilized to prognosis, treatment, medicines, and remedy, with a entire creation of HSA. This quantity will entice 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 latest wisdom of purposes of HSA and its impression on human future health in one volume.
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Extra resources for Albumin in Medicine: Pathological and Clinical Applications
This protective role of N-AcTrp can be of practical importance, because the 34Cys of HSA represents the largest fraction of free thiols in blood (Kragh-Hansen et al. 2002). In albumin products, Oct has the greatest stabilizing effect against heat, whereas the presence of N-AcTrp diminishes oxidation of HSA. 2 Important Amino Acids for the Antioxidant Activity of Marketed Albumin N-AcTrp has a possible side effect of causing intracerebral disease (Aguilera et al. 2001). In Trp metabolism, 3-hydroxykynurenine is known to have particularly strong neurotoxic properties (Topczewska-Bruns et al.
Lyophilization is known to be a suitable technique for improving the storage stability of proteins. However, dehydration during the lyophilization process sometimes causes protein denaturation and aggregation, resulting in a loss of biological activity. Sugar excipients have been widely used to stabilize the protein during lyophilization and storage (Anhorn et al. 2008). Sucrose and trehalose have also been demonstrated to be suitable stabilizers against the aggregation of rHSA (Han et al. 2007) and the other HSA fusion protein (sEphB4-HSA; discussed at Sect.
In addition to the use of sodium octanoate and N-acetyl-L-tryptophanate as a stabilizer for nanoparticles of paclitaxel, to stabilize HSA fusion proteins, ligand binding to HSA domains, genetic mutations of HSA domains, and lyophilization using sugars or surfactants are used. Keywords Human serum albumin • Thermal stability • Chemical stability • Storage stability • Stabilizer K. Yamasaki (*) • M. jp © Springer Science+Business Media Singapore 2016 M. G. 1 K. Yamasaki and M. Anraku Introduction Human serum albumin (HSA) is a major protein component of blood plasma and plays an important role in the regulation of colloidal osmotic pressure, the antioxidant capacity of human plasma, and the transport of numerous endogenous compounds such as fatty acids, hormones, toxic metabolites (eg, bilirubin), bile acids, amino acids, and metals (Peters 1995; Kragh-Hansen et al.