By Masaki Otagiri, Victor Tuan Giam Chuang
This publication provides a complete evaluation of scientific and pharmaceutical functions of human serum albumin (HSA), with updates on structural elements of albumin from the views of X-ray crystallography and NMR, endogenous and exogenous ligand binding of albumin in numerous pathological stipulations, and genetic variations and their phenotypes. quick development and improvement of its purposes have led to striking effects for which albumin has essentially been confirmed to be a powerful biomaterial. Contributions from major foreign specialists during this box exhibit how HSA is utilized to prognosis, remedy, medicinal drugs, and therapy, with a accomplished advent of HSA. This quantity will entice scientists in pharmaceutical and clinical study together with pharmaceutical chemists, pharmacokineticists, toxicologists, and biochemists not just in academia but additionally in undefined. Readers can successfully gather the newest wisdom of purposes of HSA and its effect on human health and wellbeing in one volume.
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Additional resources for Albumin in Medicine: Pathological and Clinical Applications
Compared the effects of GdnHCl-induced denaturation between mammalian (human, bovine, dog, rabbit, and rat) albumins using fluorescence and CD spectroscopies (Kosa et al. 1998). Dog albumin, which possesses a different homology in terms of the amino acid sequences in domain I, showed the highest stability against GdnHCl-induced denaturation. Thus, in addition to Cys residues that are involved in formation of disulfide bonds, several other amino acid residues located in domain I might also contribute to the stability of the molecule (Kosa et al.
Hepatol Int 10:124–132 Sudlow G, Birkett DJ, Wade DN (1975) The characterization of two speciﬁc drug binding sites on human serum albumin. 5 Å resolution. Protein Eng 12:827–835 Taguchi K, Yamasaki K, Seo H, Otagiri M (2015) Potential use of biological proteins for liver failure therapy. org. Accessed Sept 2015 Wang Z-m, Ho JX, Ruble JR, Rose J, Rüker F, Ellenburg M, Murphy R, Click J, Soistman E, Wilkerson L, Carter DC (2013) Structural studies of several clinically important oncology drugs in complex with human serum albumin.
4). For the formulations of these new products, more research directed at identifying factors that affect the stability of such molecules will be highly desirable. 6 Conclusion and Future Prospects The identification of factors that affect the structures of HSA (ie, heat, chemicals, and genetic variations) helps not only to explain the dynamic structure of this protein but also to identify the important positions on the molecule (ie, domains or amino acid residues) that affect its stability, which finally serves to predict the stability of HSA at the point of production and storage.
Albumin in Medicine: Pathological and Clinical Applications by Masaki Otagiri, Victor Tuan Giam Chuang