Considerations on Probe Design for Affinity-Guided Protein Conjugation

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

DOI

  • Michael R. Mortensen, Center for Multifunctional Biomolecular Drug Design at the Interdisciplinary Nanoscience Center
  • ,
  • Mikkel B. Skovsgaard, Center for Multifunctional Biomolecular Drug Design at the Interdisciplinary Nanoscience Center
  • ,
  • Kurt V. Gothelf
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.
OriginalsprogEngelsk
TidsskriftChemBioChem
Vol/bind20
Nummer21
Sider (fra-til)2711-2728
Antal sider18
ISSN1439-4227
DOI
StatusUdgivet - nov. 2019

Se relationer på Aarhus Universitet Citationsformater

ID: 171396695