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Designed Ankyrin Repeat Proteins (DARPins)


Tamaskovic, Rastislav; Simon, Manuel; Stefan, Nikolas; Schwill, Martin; Plückthun, Andreas (2012). Designed Ankyrin Repeat Proteins (DARPins). Methods in Enzymology, 503:101-134.

Abstract

Designed ankyrin repeat proteins (DARPins) have been developed into a robust and versatile scaffold for binding proteins. High-affinity binders are routinely selected by ribosome display and phage display. DARPins have entered clinical trials and have found numerous uses in research, due to their high stability and robust folding, allowing many new molecular formats. We summarize the DARPin properties and highlight some biomedical applications. Protocols are given for labeling with dyes and polyethylene glycol, for quantitatively measuring binding to cell surface receptors by kinetics and thermodynamics, and for exploiting new engineering opportunities from using "click chemistry" with nonnatural amino acids.

Abstract

Designed ankyrin repeat proteins (DARPins) have been developed into a robust and versatile scaffold for binding proteins. High-affinity binders are routinely selected by ribosome display and phage display. DARPins have entered clinical trials and have found numerous uses in research, due to their high stability and robust folding, allowing many new molecular formats. We summarize the DARPin properties and highlight some biomedical applications. Protocols are given for labeling with dyes and polyethylene glycol, for quantitatively measuring binding to cell surface receptors by kinetics and thermodynamics, and for exploiting new engineering opportunities from using "click chemistry" with nonnatural amino acids.

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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > Department of Biochemistry
07 Faculty of Science > Department of Biochemistry
Dewey Decimal Classification:570 Life sciences; biology
Scopus Subject Areas:Life Sciences > Biochemistry
Life Sciences > Molecular Biology
Language:English
Date:2012
Deposited On:11 Oct 2012 09:09
Last Modified:23 Jan 2022 22:29
Publisher:Elsevier
ISSN:0076-6879
OA Status:Closed
Publisher DOI:https://doi.org/10.1016/B978-0-12-396962-0.00005-7
PubMed ID:22230567