2014•Bioconjugate ChemistryRequires access

Switchavidin: Reversible Biotin–Avidin–Biotin Bridges with High Affinity and Specificity

Barbara Taskinen, Dominik Zauner, Soili I. Lehtonen, Masi Koskinen, Chloe Thomson, Niklas Kähkönen, Sampo Kukkurainen, Juha A. E. Määttä, Teemu O. Ihalainen, Markku S. Kulomaa, Hermann J. Gruber, Vesa Pekka Hytönen

Open publisher page 36 citations

Abstract

Switchavidin is a chicken avidin mutant displaying reversible binding to biotin, an improved binding affinity toward conjugated biotin, and low nonspecific binding due to reduced surface charge. These properties make switchavidin an optimal tool in biosensor applications for the reversible immobilization of biotinylated proteins on biotinylated sensor surfaces. Furthermore, switchavidin opens novel possibilities for patterning, purification, and labeling.

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What this paper is about

Switchavidin is a chicken avidin mutant displaying reversible binding to biotin, an improved binding affinity toward conjugated biotin, and low nonspecific binding due to reduced surface charge. These properties make switchavidin an optimal tool in biosensor applications for the reversible immobilization of biotinylated proteins on biotinylated sensor surfaces. Furthermore, switchavidin opens novel possibilities for patterning, purification, and labeling.

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OpenAlex reports 36 citations for this work. Citation counts describe recorded attention and do not establish research quality.

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Available abstract

Switchavidin is a chicken avidin mutant displaying reversible binding to biotin, an improved binding affinity toward conjugated biotin, and low nonspecific binding due to reduced surface charge. These properties make switchavidin an optimal tool in biosensor applications for the reversible immobilization of biotinylated proteins on biotinylated sensor surfaces. Furthermore, switchavidin opens novel possibilities for patterning, purification, and labeling.

Key concepts: Biotinylation, Avidin, Biotin, Chemistry, Streptavidin, Biosensor, Biochemistry, Mutant

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