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Bispecific applications of non-immunoglobulin scaffold binders
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Protein Science.ORCID iD: 0000-0003-0605-8417
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Protein Science, Protein Technology.
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Protein Science.ORCID iD: 0000-0002-6104-6446
2019 (English)In: Methods, ISSN 1046-2023, E-ISSN 1095-9130, Vol. 154, p. 143-152Article in journal (Refereed) Published
Abstract [en]

Non-immunoglobulin scaffolds represent a proven group of small affinity proteins that can be engineered in vitro to similar affinity and potency as monoclonal antibodies. Several novel candidate biotherapeutics that exploit the potential advantages scaffold proteins hold over larger and more complex antibodies have been developed over the past decade. The ease of using small and robust binding proteins as flexible and modular building blocks has led to the development of a wide range of innovative approaches to combine them in various bi- and multispecific formats. This progress is expected to aid the ongoing challenge of identifying niche applications where clear differentiation from antibody-based molecules will be key to success. Given the many engineering options that are available for non-immunoglobulin scaffold proteins, they have potential to not only complement but probably also surpass antibodies in certain applications.

Place, publisher, year, edition, pages
ACADEMIC PRESS INC ELSEVIER SCIENCE , 2019. Vol. 154, p. 143-152
Keywords [en]
Non-immunoglobulin scaffold, In vitro evolution, Protein engineering, Bispecific, Biparatopic
National Category
Other Industrial Biotechnology
Identifiers
URN: urn:nbn:se:kth:diva-244538DOI: 10.1016/j.ymeth.2018.09.010ISI: 000457813100017PubMedID: 30287281Scopus ID: 2-s2.0-85054456517OAI: oai:DiVA.org:kth-244538DiVA, id: diva2:1302167
Note

QC 20190403

Available from: 2019-04-03 Created: 2019-04-03 Last updated: 2019-08-30Bibliographically approved

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Hober, SophiaLindbo, SarahNilvebrant, Johan

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