Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 58, Issue 25, Pages 8278-8290Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201811293
Keywords
chemical biology; fluorescence microscopy; metal-chelating complexes; protein labeling; super-resolution microscopy
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Funding
- German Research Foundation [GRK 1986, SFB 807, EXC 114]
- LOEWE Program DynaMem
- Volkswagen Foundation [91 068, 91 067]
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With the advent of single-molecule methods, chemoselective and site-specific labeling of proteins evolved to become a central aspect in chemical biology as well as cell biology. Protein labeling demands high specificity, rapid as well as efficient conjugation, while maintaining low concentration and biocompatibility under physiological conditions. Generic methods that do not interfere with the function, dynamics, subcellular localization of proteins, and crosstalk with other factors are crucial to probe and image proteins invitro and in living cells. Alternatives to enzyme-based tags or autofluorescent proteins are short peptide-based recognition tags. These tags provide high specificity, enhanced binding rates, bioorthogonality, and versatility. Here, we report on recent applications of multivalent chelator heads, recognizing oligohistidine-tagged proteins. The striking features of this system has facilitated the analysis of protein complexes by single-molecule approaches.
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