Switchavidin: reversible biotin-avidin-biotin bridges with high affinity and specificity

Barbara Taskinen; Dominik Zauner; S. I. Lehtonen; M. Koskinen; C. Thomson; N. Kähkönen; S. Kukkurainen; J. A. E. Määttä; T. O. Ihalainen; M. S. Kulomaa; Hermann Gruber; V. P. Hytonen

doi:10.1021/bc500462w

Switchavidin: reversible biotin-avidin-biotin bridges with high affinity and specificity

Barbara Taskinen, Dominik Zauner, S. I. Lehtonen, M. Koskinen, C. Thomson, N. Kähkönen, S. Kukkurainen, J. A. E. Määttä, T. O. Ihalainen, M. S. Kulomaa, Hermann Gruber, V. P. Hytonen

Department of Molecular and Membrane Biophysics

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	2233-2243
Number of pages	11
Journal	Bioconjugate Chemistry
Volume	25
Issue number	12
DOIs	https://doi.org/10.1021/bc500462w
Publication status	Published - 2014

Fields of science

103 Physics, Astronomy
106006 Biophysics

JKU Focus areas

Engineering and Natural Sciences (in general)

Access to Document

10.1021/bc500462w

Cite this

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title = "Switchavidin: reversible biotin-avidin-biotin bridges with high affinity and specificity",

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.",

author = "Barbara Taskinen and Dominik Zauner and Lehtonen, {S. I.} and M. Koskinen and C. Thomson and N. K{\"a}hk{\"o}nen and S. Kukkurainen and M{\"a}{\"a}tt{\"a}, {J. A. E.} and Ihalainen, {T. O.} and Kulomaa, {M. S.} and Hermann Gruber and Hytonen, {V. P.}",

year = "2014",

doi = "10.1021/bc500462w",

language = "English",

volume = "25",

pages = "2233--2243",

journal = "Bioconjugate Chemistry",

issn = "1520-4812",

publisher = "American Chemical Society",

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T1 - Switchavidin: reversible biotin-avidin-biotin bridges with high affinity and specificity

AU - Taskinen, Barbara

AU - Zauner, Dominik

AU - Lehtonen, S. I.

AU - Koskinen, M.

AU - Thomson, C.

AU - Kähkönen, N.

AU - Kukkurainen, S.

AU - Määttä, J. A. E.

AU - Ihalainen, T. O.

AU - Kulomaa, M. S.

AU - Gruber, Hermann

AU - Hytonen, V. P.

PY - 2014

Y1 - 2014

N2 - 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.

AB - 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.

U2 - 10.1021/bc500462w

DO - 10.1021/bc500462w

M3 - Article

SN - 1520-4812

VL - 25

SP - 2233

EP - 2243

JO - Bioconjugate Chemistry

JF - Bioconjugate Chemistry

IS - 12

ER -