Detection of the PRAME Protein on the Surface of Melanoma Cells Using a Fluorescently Labeled Monoclonal Antibody

Detection of the PRAME Protein on the Surface of Melanoma Cells Using a Fluorescently Labeled Monoclonal Antibody

Determination of the expression level of tumor marker PRAME protein is important both for predicting the course of the disease and for monitoring the effectiveness of anticancer therapy. A fluorescently labeled monoclonal antibody to the PRAME protein was obtained by periodate oxidation of glycans f...

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Bibliographic Details
Published in:Russian journal of bioorganic chemistry Vol. 47; no. 5; pp. 1077 - 1085
Main Authors: Sapozhnikova, K. A., Misyurin, A. V., Pestov, N. B., Meleshkina, E. G., Oreshkov, S. D., Ganzhula, E. P., Mikhailova, A. S., Korshun, V. A., Misyurin, V. A., Brylev, V. A.
Format: Journal Article
Language:English
Published: Moscow Pleiades Publishing 01-09-2021
Springer Nature B.V
Subjects:
Absorption spectra
Alkynes
Anticancer properties
Biochemistry
Biomedical and Life Sciences
Biomedicine
Bioorganic Chemistry
Cancer
Cyanine dyes
Fluorescence
Life Sciences
Markers
Monoclonal antibodies
Organic Chemistry
Oxidation
Proteins
Reagents
Stoichiometry
“click” reaction
monoclonal antibody
fluorescent label
oxyamine
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Summary:Determination of the expression level of tumor marker PRAME protein is important both for predicting the course of the disease and for monitoring the effectiveness of anticancer therapy. A fluorescently labeled monoclonal antibody to the PRAME protein was obtained by periodate oxidation of glycans followed by modification with a bifunctional azido-oxyamine reagent and a “click” reaction with alkyne-modified sulfonated cyanine dye Cy3. A new approach to the synthesis of a bifunctional azido-oxyamine reagent using the ethoxyethylidene protecting group for oxyamine is proposed. The labeled antibodies were characterized with UV/Vis absorption spectra and the stoichiometry of the modification was determined. It has been demonstrated that the fluorescent antibodies retain affinity and can be used as a diagnostic tool for detecting the residual marker (the PRAME protein) after anticancer therapy.
ISSN:1068-1620
1608-330X
DOI:10.1134/S1068162021050332