Pharmaceutically Important Pre- and Posttranslational Modifications on Human Serum Albumin

• Otagiri Masaki

  Department of Biopharmaceutics, Graduate School of Pharmaceutical Sciences, Kumamoto University

• Chuang Victor Tuan Giam

  Department of Biopharmaceutics, Graduate School of Pharmaceutical Sciences, Kumamoto University School of Pharmacy, Curtin University of Technology

Abstract

Recombinant technology allows engineering and production of proteins with desirable properties. Human serum albumin has been developed with recombinant technology, and thus plays an increasing role as a drug carrier in the clinical setting. Genetic variations usually occur on the surface of the protein, and do not impose significant effects on the conformation of albumin. However, binding of fatty acids by genetic variants is affected according to the location of the mutation. Albumin undergoes three major posttranslational modifications, namely, oxidation, glycation, and S-nitrosylation. This review gives an account of the different posttranslational modifications that should be taken into consideration when designing albumin mutant analogues with desirable pharmaceutical properties.

Journal

• Biological and Pharmaceutical Bulletin

  Biological and Pharmaceutical Bulletin 32 (4), 527-534, 2009

  The Pharmaceutical Society of Japan

Keywords

• human serum albumin
• genetic variant
• posttranslational modification: oxidation
• glycation
• <i>S</i>-nitrosylation

Details

• CRID: 1390282679601139840
• NII Article ID: 110007160707
• NII Book ID: AA10885497
• DOI: 10.1248/bpb.32.527
• ISSN: 13475215
• ISSN: 09186158
• NDL BIB ID: 10194129
• Web Site: http://id.ndl.go.jp/bib/10194129
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I10194129
• Web Site: http://www.jstage.jst.go.jp/article/bpb/32/4/32_4_527/_pdf
• Web Site: https://search.jamas.or.jp/link/ui/2009266092
• Text Lang: en
• Data Source:
  • JaLC
  • NDL
  • Crossref
  • CiNii Articles
• Abstract License Flag: Disallowed