Engineered affinity proteins-Generation and applications
2009 (English)In: Journal of Biotechnology, ISSN 0168-1656, E-ISSN 1873-4863, Vol. 140, no 3-4, 254-269 p.Article, review/survey (Refereed) Published
The use of combinatorial protein engineering to design proteins with novel binding specificities and desired properties has evolved into a powerful technology, resulting in the recent advances in protein library selection strategies and the emerge of a variety of new engineered affinity proteins. The need for different protein library selection methods is due to that each target protein pose different challenges in terms of its availability and inherent properties. At present, alternative engineered affinity proteins are starting to complement and even challenge the classical immunoglobulins in different applications in biotechnology and potentially also for in vivo use as imaging agents or as biotherapeutics. This review article covers the generation and use of affinity proteins generated through combinatorial protein engineering. The most commonly used selection techniques for isolation of desired variants from large protein libraries are described. Different antibody derivatives, as well as a variety of the most validated engineered protein scaffolds, are discussed. In addition, we provide an overview of some of the major present and future applications for these engineered affinity proteins in biotechnology and medicine.
Place, publisher, year, edition, pages
2009. Vol. 140, no 3-4, 254-269 p.
Affinity protein, Combinatorial protein engineering, Molecular, recognition, Selection method, Protein library, Protein scaffold, ankyrin repeat protein, yeast surface display, in-vitro selection, combinatorial antibody libraries, alternative binding-proteins, bacterial receptor domain, growth-factor receptor, messenger-rna, display, taq dna-polymerase, phage display
IdentifiersURN: urn:nbn:se:kth:diva-18362DOI: 10.1016/j.jbiotec.2009.01.014ISI: 000265465500016OAI: oai:DiVA.org:kth-18362DiVA: diva2:336408
QC 201005252010-08-052010-08-052010-12-22Bibliographically approved