A nonavalent BODIPY with a multivalent arrangement of α-mannosides enables lectins recognition in fluorescence-based assays

We report here the use of Tris-BODIPY-OH as a scaffold for the multivalent display of sugar heads. A chloroacetyl thioether ligation reaction easily yields mannosylated BODIPYs, named Man<sub>9</sub>-BODIPY and (Man-TEG)<sub>9</sub>-BODIPY, which display nine mannose residues. Regardless of the linker length, both glycoBODIPYs provide an arrangement of mannose heads that allows for proper recognition by the carbohydrate binding domain of concanavalin A (ConA). Moreover, the interactions of Man<sub>9</sub>-BODIPY with relevant human lectins, <i>i.e.</i> dendritic cell-specific intercellular adhesion molecule-3-grabbing non-integrin (DC-SIGN) and langerin, were further investigated. The approach proposed is versatile and paves the way for the development of multivalent and fluorescent glyco-BODIPY probes useful to interrogate carbohydrate-lectin interactions in different biological contexts.

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Publication Details

Journal
RSC Chemical Biology
Published
2025-12-05
DOI
https://doi.org/10.1039/d5cb00190k
Primary Topic
Luminescence and Fluorescent Materials
Type
article
Field-Weighted Citation Impact
0.00

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article

A nonavalent BODIPY with a multivalent arrangement of α-mannosides enables lectins recognition in fluorescence-based assays

Giacomo Biagiotti, Yvette van Kooyk, Stefano Cicchi, Jacopo Tricomi et al.
RSC Chemical Biology
Luminescence and Fluorescent Materials
article

A nonavalent BODIPY with a multivalent arrangement of α-mannosides enables lectins recognition in fluorescence-based assays

Giacomo Biagiotti, Yvette van Kooyk, Stefano Cicchi, Jacopo Tricomi, Marko Anderluh, Janez Mravljak, Marco Laurati, Iztok Urbančič, Barbara Richichi, Fabrizio Chiodo, Edvin Purić
article en

Abstract

We report here the use of Tris-BODIPY-OH as a scaffold for the multivalent display of sugar heads. A chloroacetyl thioether ligation reaction easily yields mannosylated BODIPYs, named Man<sub>9</sub>-BODIPY and (Man-TEG)<sub>9</sub>-BODIPY, which display nine mannose residues. Regardless of the linker length, both glycoBODIPYs provide an arrangement of mannose heads that allows for proper recognition by the carbohydrate binding domain of concanavalin A (ConA). Moreover, the interactions of Man<sub>9</sub>-BODIPY with relevant human lectins, <i>i.e.</i> dendritic cell-specific intercellular adhesion molecule-3-grabbing non-integrin (DC-SIGN) and langerin, were further investigated. The approach proposed is versatile and paves the way for the development of multivalent and fluorescent glyco-BODIPY probes useful to interrogate carbohydrate-lectin interactions in different biological contexts.

RSC Chemical BiologyVol. 7(3)
University of Ljubljana (SI), Jožef Stefan Institute (SI), Consorzio Interuniversitario per lo Sviluppo dei Sistemi a Grande Interfase (IT), National Research Council (IT), University of Florence (IT), Vrije Universiteit Amsterdam (NL)
Dipartimenti di Eccellenza, European Commission, Javna Agencija za Raziskovalno Dejavnost RS, Università degli Studi di Firenze, European Regional Development Fund
Openalex Percentile: Top 68%
Luminescence and Fluorescent Materials
DOIOpen Access PDFOpenAlex
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