Considerations on Probe Design for Affinity-Guided Protein Conjugation

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Considerations on Probe Design for Affinity-Guided Protein Conjugation. / Mortensen, Michael R.; Skovsgaard, Mikkel B.; Gothelf, Kurt V.

I: ChemBioChem, Bind 20, Nr. 21, 11.2019, s. 2711-2728.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisReviewForskningpeer review

Harvard

Mortensen, MR, Skovsgaard, MB & Gothelf, KV 2019, 'Considerations on Probe Design for Affinity-Guided Protein Conjugation', ChemBioChem, bind 20, nr. 21, s. 2711-2728. https://doi.org/10.1002/cbic.201900157

APA

CBE

MLA

Mortensen, Michael R., Mikkel B. Skovsgaard, og Kurt V. Gothelf. "Considerations on Probe Design for Affinity-Guided Protein Conjugation". ChemBioChem. 2019, 20(21). 2711-2728. https://doi.org/10.1002/cbic.201900157

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Author

Mortensen, Michael R. ; Skovsgaard, Mikkel B. ; Gothelf, Kurt V. / Considerations on Probe Design for Affinity-Guided Protein Conjugation. I: ChemBioChem. 2019 ; Bind 20, Nr. 21. s. 2711-2728.

Bibtex

@article{ee26a3e29c3144e3b84d897870837e2b,
title = "Considerations on Probe Design for Affinity-Guided Protein Conjugation",
abstract = "The plethora of methods developed for the creation of protein conjugates often differs significantly with regard to the heterogeneity of the resulting products, in the degree of genetic manipulation of the protein required, and in the technical skills required to perform the conjugation procedure. Affinity-guided protein conjugation is a protein labeling methodology based on noncovalent binding interactions between a labeling probe and the protein of interest. These interactions increase the local concentration of a reactive group in the probe on the protein surface thus facilitating the conjugation in proximity of the complexation site. The ability to produce high-quality conjugates from nongenetically modified proteins both in vitro, but also in cells, demonstrates the power of affinity-guided protein conjugation. Here, we present the progress of affinity-guided protein conjugation in relation to selective protein labeling in living systems and the formation of high-quality protein conjugates. Furthermore, the probe design will be discussed in relation to the utility of the probe for labeling in vitro or in living systems.",
keywords = "affinity-guided conjugation, live-cell labeling, protein conjugation, proximity ligation, site-selective protein modification",
author = "Mortensen, {Michael R.} and Skovsgaard, {Mikkel B.} and Gothelf, {Kurt V.}",
year = "2019",
month = nov,
doi = "10.1002/cbic.201900157",
language = "English",
volume = "20",
pages = "2711--2728",
journal = "ChemBioChem",
issn = "1439-4227",
publisher = "Wiley - V C H Verlag GmbH & Co. KGaA",
number = "21",

}

RIS

TY - JOUR

T1 - Considerations on Probe Design for Affinity-Guided Protein Conjugation

AU - Mortensen, Michael R.

AU - Skovsgaard, Mikkel B.

AU - Gothelf, Kurt V.

PY - 2019/11

Y1 - 2019/11

N2 - The plethora of methods developed for the creation of protein conjugates often differs significantly with regard to the heterogeneity of the resulting products, in the degree of genetic manipulation of the protein required, and in the technical skills required to perform the conjugation procedure. Affinity-guided protein conjugation is a protein labeling methodology based on noncovalent binding interactions between a labeling probe and the protein of interest. These interactions increase the local concentration of a reactive group in the probe on the protein surface thus facilitating the conjugation in proximity of the complexation site. The ability to produce high-quality conjugates from nongenetically modified proteins both in vitro, but also in cells, demonstrates the power of affinity-guided protein conjugation. Here, we present the progress of affinity-guided protein conjugation in relation to selective protein labeling in living systems and the formation of high-quality protein conjugates. Furthermore, the probe design will be discussed in relation to the utility of the probe for labeling in vitro or in living systems.

AB - The plethora of methods developed for the creation of protein conjugates often differs significantly with regard to the heterogeneity of the resulting products, in the degree of genetic manipulation of the protein required, and in the technical skills required to perform the conjugation procedure. Affinity-guided protein conjugation is a protein labeling methodology based on noncovalent binding interactions between a labeling probe and the protein of interest. These interactions increase the local concentration of a reactive group in the probe on the protein surface thus facilitating the conjugation in proximity of the complexation site. The ability to produce high-quality conjugates from nongenetically modified proteins both in vitro, but also in cells, demonstrates the power of affinity-guided protein conjugation. Here, we present the progress of affinity-guided protein conjugation in relation to selective protein labeling in living systems and the formation of high-quality protein conjugates. Furthermore, the probe design will be discussed in relation to the utility of the probe for labeling in vitro or in living systems.

KW - affinity-guided conjugation

KW - live-cell labeling

KW - protein conjugation

KW - proximity ligation

KW - site-selective protein modification

UR - http://www.scopus.com/inward/record.url?scp=85068087309&partnerID=8YFLogxK

U2 - 10.1002/cbic.201900157

DO - 10.1002/cbic.201900157

M3 - Review

C2 - 30983114

AN - SCOPUS:85068087309

VL - 20

SP - 2711

EP - 2728

JO - ChemBioChem

JF - ChemBioChem

SN - 1439-4227

IS - 21

ER -