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Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of GoldIII
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Protein labelling and albumin binding characteristics of the near-IR Cy7 fluorophore, QuatCy

Sopida Thavornpradit1, Syed Muhammad Usama1, Chen-Ming Lin1

  • 1Department of Chemistry, Texas A & M University, Box 30012, College Station, TX 77842, USA. burgess@tamu.edu.

Organic & Biomolecular Chemistry
|July 19, 2019
PubMed

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.

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