Protein labelling and albumin binding characteristics of the near-IR Cy7 fluorophore, QuatCy. Issue 30 (18th July 2019)

• Record Type: Journal Article
• Authors: Thavornpradit, Sopida; Usama, Syed Muhammad; Lin, Chen-Ming; Burgess, Kevin
• Is Part Of: Organic & biomolecular chemistry. Volume 17:Issue 30(2019)
• Page Start: 7150
• Page End: 7154
• Publication Date: 2019-07-18
• Subjects: Chemistry, Organic -- Periodicals; Bioorganic chemistry -- Periodicals; Chemistry, Physical organic -- Periodicals; 547
• DOI: 10.1039/c9ob01184f
• Languages: English
• ISSNs: 1477-0520

Abstract

Abstract : "QuatCy" selectively labels Cys side-chains, and proteins with exposed Cys residues over albumin. 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.