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

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.

authors

• Burgess, Kevin

published proceedings

• Org Biomol Chem

author list (cited authors)

• Thavornpradit, S., Usama, S. M., Lin, C., & Burgess, K.

citation count

• 9

complete list of authors

• Thavornpradit, Sopida||Usama, Syed Muhammad||Lin, Chen-Ming||Burgess, Kevin

publication date

• August 2019

publisher

• Royal Society of Chemistry (RSC)  Publisher

published in

• Organic and Biomolecular Chemistry  Journal

keywords

• Binding Sites
• Carbocyanines
• Fluorescent Dyes
• Humans
• Infrared Rays
• Molecular Structure
• Optical Imaging
• Serum Albumin, Human

PubMed Central ID

• 31317168

Digital Object Identifier (DOI)

• 10.1039/c9ob01184f

start page

• 7150

end page

• 7154

volume

• 17

issue

• 30