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

Org Biomol Chem. 2019 Aug 14;17(30):7150-7154. doi: 10.1039/c9ob01184f. Epub 2019 Jul 18.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Binding Sites
  • Carbocyanines / chemical synthesis
  • Carbocyanines / chemistry*
  • Fluorescent Dyes / chemical synthesis
  • Fluorescent Dyes / chemistry*
  • Humans
  • Infrared Rays
  • Molecular Structure
  • Optical Imaging
  • Serum Albumin, Human / chemistry*

Substances

  • Carbocyanines
  • Fluorescent Dyes
  • Serum Albumin, Human