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Polyionic and cysteine-containing fusion peptides as versatile protein tags
Umeå University, Faculty of Science and Technology, Department of Chemistry.
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2013 (English)In: Biological chemistry (Print), ISSN 1431-6730, E-ISSN 1437-4315, Vol. 394, no 8, 995-1004 p.Article, review/survey (Refereed) Published
Abstract [en]

In response to advances in proteomics research and the use of proteins in medical and biotechnological applications, recombinant protein production and the design of specific protein characteristics and functions has become a widely used technology. In this context, protein fusion tags have been developed as indispensable tools for protein expression, purification, and the design of functionalized surfaces or artificially bifunctional proteins. Here we summarize how positively or negatively charged polyionic fusion peptides with or without an additional cysteine can be used as protein tags for protein expression and purification, for matrix-assisted refolding of aggregated protein, and for coupling of proteins either to technologically relevant matrices or to other proteins. In this context we used cysteine-containing polyionic fusion peptides for the design of immunotoxins. In general, polyionic fusion tags can be considered as a multifunctional module in protein technology.

Place, publisher, year, edition, pages
2013. Vol. 394, no 8, 995-1004 p.
Keyword [en]
bifunctional proteins, disulfide bonds, immunotoxins, polyionic interactions, protein purification, renaturation
National Category
Cell and Molecular Biology
URN: urn:nbn:se:umu:diva-79226DOI: 10.1515/hsz-2013-0116ISI: 000321255100007OAI: diva2:648503
Available from: 2013-09-16 Created: 2013-08-13 Last updated: 2013-09-26Bibliographically approved

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Frost, Stefan
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