Alternative binding proteins: Affibody binding proteins developed from a small three-helix bundle scaffold

249Citations
Citations of this article
283Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

In recent years, classical antibody-based affinity reagents have been challenged by novel types of binding proteins developed by combinatorial protein engineering principles. One of these classes of binding proteins of non-Ig origin are the so-called affibody binding proteins, functionally selected from libraries of a small (6 kDa), non-cysteine three-helix bundle domain used as a scaffold. During the first 10 years since they were first described, high-affinity affibody binding proteins have been selected towards a large number of targets for use in a variety of applications, such as bioseparation, diagnostics, functional inhibition, viral targeting and in vivo tumor imaging/therapy. The small size offers the possibility to produce functional affibody binding proteins also by chemical synthesis production routes, which has been found to be advantageous for the site-specific introduction of various labels and radionuclide chelators. © 2008 The Author.

Cite

CITATION STYLE

APA

Nygren, P. Å. (2008, June). Alternative binding proteins: Affibody binding proteins developed from a small three-helix bundle scaffold. FEBS Journal. https://doi.org/10.1111/j.1742-4658.2008.06438.x

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free