ArticleOrganic & biomolecular chemistry2019
Protein labelling and albumin binding characteristics of the near-IR Cy7 fluorophore, QuatCy.
Article in Organic & biomolecular chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Cyanidin-3-O-glucoside (C3G): A natural small-molecule compound for alleviating envenomation symptoms Induced by Bungarus multicinctus.PLoS neglected tropical diseases · 2026Article
- Recent advances in targeting cyanine dyes: hierarchical targeting mechanisms and theranostic integration for multi-disease precision therapy.Theranostics · 2026Review
- Visual Tracking and Organ Targeting ofToxins · 2025Article
- Albumin Encapsulation of Cyanine Dye for High-Performance NIR-II Imaging-Guided Photodynamic Therapy.Chemical & biomedical imaging · 2025Article
- Tracking the Fate of Therapeutic Proteins Using Ratiometric Imaging of Responsive Shortwave Infrared Probes.Journal of the American Chemical Society · 2025Article
- Site-specific albumin tagging with NIR-II fluorogenic dye for high-performance and super-stable bioimaging.Theranostics · 2024Article
- Albumin-seeking dyes with adjustable assembliesTheranostics · 2024Article
- Cytotoxicities of Tumor-Seeking Dyes: Impact on Future Clinical Trials.ChemMedChem · 2023Article
- Multifunctional Near-Infrared Dye IR-817 Encapsulated in Albumin Nanoparticles for Enhanced Imaging and Photothermal Therapy in Melanoma.International journal of nanomedicine · 2023Article
- Unraveling the Chemistry ofACS bio & med chem Au · 2022Article
- Conjugation of Palbociclib with MHI-148 Has an Increased Cytotoxic Effect for Breast Cancer Cells and an Altered Mechanism of Action.Molecules (Basel, Switzerland) · 2022Article
- Super-stable cyanine@albumin fluorophore for enhanced NIR-II bioimaging.Theranostics · 2022Article
- Role of Albumin in Accumulation and Persistence of Tumor-Seeking Cyanine Dyes.Bioconjugate chemistry · 2020Article
Corrections and comments
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Authors and funding
4 authors.
Funding
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.
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