Amine Landscaping to Maximize Protein-Dye Fluorescence and Ultrastable Protein-Ligand Interaction
Cell Chemical Biology, ISSN: 2451-9456, Vol: 24, Issue: 8, Page: 1040-1047.e4
2017
- 14Citations
- 79Captures
- 4Mentions
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations14
- Citation Indexes14
- 14
- CrossRef11
- Captures79
- Readers79
- 79
- Mentions4
- References4
- Wikipedia4
Article Description
Chemical modification of proteins provides great opportunities to control and visualize living systems. The most common way to modify proteins is reaction of their abundant amines with N-hydroxysuccinimide (NHS) esters. Here we explore the impact of amine number and positioning on protein-conjugate behavior using streptavidin-biotin, a central research tool. Dye-NHS modification of streptavidin severely damaged ligand binding, necessitating development of a new streptavidin-retaining ultrastable binding after labeling. Exploring the ideal level of dye modification, we engineered a panel bearing 1–6 amines per subunit: “amine landscaping.” Surprisingly, brightness increased as amine number decreased, revealing extensive quenching following conventional labeling. We ultimately selected Flavidin (fluorophore-friendly streptavidin), combining ultrastable ligand binding with increased brightness after conjugation. Flavidin enhanced fluorescent imaging, allowing more sensitive and specific cell labeling in tissues. Flavidin should have wide application in molecular detection, providing a general insight into how to optimize simultaneously the behavior of the biomolecule and the chemical probe.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S2451945617302295; http://dx.doi.org/10.1016/j.chembiol.2017.06.015; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85026225827&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/28757182; https://linkinghub.elsevier.com/retrieve/pii/S2451945617302295; https://dx.doi.org/10.1016/j.chembiol.2017.06.015
Elsevier BV
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