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Affinity proteins and their generation
KTH, Skolan för bioteknologi (BIO), Molekylär Bioteknologi.ORCID-id: 0000-0002-9282-0174
KTH, Skolan för bioteknologi (BIO), Molekylär Bioteknologi.
KTH, Skolan för bioteknologi (BIO), Molekylär Bioteknologi.ORCID-id: 0000-0001-9423-0541
2013 (engelsk)Inngår i: Journal of chemical technology and biotechnology (1986), ISSN 0268-2575, E-ISSN 1097-4660, Vol. 88, nr 1, s. 25-38Artikkel, forskningsoversikt (Fagfellevurdert) Published
Abstract [en]

Engineered affinity proteins have, together with antibodies and antibody derivatives, become indispensable tools in many areas of life science and with an increasing number of applications. The need for high-throughput methods for generation of these different affinity proteins is evident. Today, combinatorial protein engineering is the most successful strategy to generate novel affinity proteins of non-immunoglobulin origin. In this approach, high-complexity combinatorial libraries are constructed from which affinity proteins are isolated using appropriate selection methods, thus circumventing the need for detailed knowledge of the protein structure and the binding mechanism that is necessary in more rational approaches. Since the introduction of the phage display technology, several alternative selection systems have been developed for this purpose. This review presents briefly some of the more commonly used affinity proteins, and gives an overview of the different methods and challenges related to the generation of library diversity and the selection methods available for the isolation of affinity proteins with desired properties.

sted, utgiver, år, opplag, sider
2013. Vol. 88, nr 1, s. 25-38
Emneord [en]
Affinity proteins, Cell surface display, Combinatorial library, Directed evolution, Phage display, Protein engineering, Scaffold proteins, Selection systems
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Identifikatorer
URN: urn:nbn:se:kth:diva-117828DOI: 10.1002/jctb.3929ISI: 000313944000004Scopus ID: 2-s2.0-84870851878OAI: oai:DiVA.org:kth-117828DiVA, id: diva2:603240
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QC 20130205

Tilgjengelig fra: 2013-02-05 Laget: 2013-02-05 Sist oppdatert: 2017-12-06bibliografisk kontrollert

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