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Protein labelling and albumin binding characteristics of the near-IR Cy7 fluorophore, QuatCy†
Sopida Thavornpradit,Syed Muhammad Usama,Chen-Ming Lin,Kevin Burgess
Organic & Biomolecular Chemistry Pub Date : 07/18/2019 00:00:00 , DOI:10.1039/C9OB01184F
Abstract

Free cysteine residues react with QuatCy 1, by simply mixing the protein and dye in aqueous buffer at 37 °C. Another dye, MHI-148, can be used for a similar labelling protocol, but QuatCy reacts faster with all proteins studied, except albumin; it emerges here that this is because MHI-148 instantly forms of a non-covalent complex with albumin, but QuatCy does not. Labelling with QuatCy has advantages insofar as it is over five times brighter, and much more photostable, than MHI-148, and combination labelling with this dye pair will allow multiplexing in the near-IR region.

Graphical abstract: Protein labelling and albumin binding characteristics of the near-IR Cy7 fluorophore, QuatCy
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