Abstract
A concise synthetic route from methylmalonate to a tetravalent aliphatic scaffold has been developed. The ensuing tetra-tethered derivative is equipped with two hydroxyl groups, as well as orthogonal alkene and alkyne functionalities. The usefulness of the scaffold has been demonstrated with the preparation of two representative multivalent derivatives: (i) a tetravalent compound containing two D-mannose units, one fluorescent boron-dipyrromethene (BODIPY) dye and a suitably functionalized amino acid and (ii) by way of dimerization and saponification, a water-soluble tetramannan derivative containing two fluorescent BODIPY units. Additionally, photophysical measurements conducted on these derivatives support the viability of the herein designed single and double BODIPY-labeled carbohydrate-based clusters as fluorescent markers.
Highlights
It is currently accepted that a broad range of biological functions is associated with recognition events between carbohydrates and proteins [1,2]
A further refinement related to the aforementioned carbohydrate-protein interactions came with the realization that individual carbohydrate-ligands bind to a protein site weakly, and the high levels of recognition in biological events had to be associated to the existence of the so-called multivalent interactions [25]. In these interactions, multiple copies of the ligands and receptors must be involved in the binding event in order to provide the significantly high levels of specificity required for the biological processes to take place [26,27,28]
(4) with pentenyl bromide and propargyl bromide paved the way to, previously dimethyl malonate with pentenyl bromide and propargyl bromide paved the way to, previously dimethyl malonate with pentenyl bromide propargyl bromide paved the way to, previously unreported, ene-yne(4)derivative
Summary
It is currently accepted that a broad range of biological functions is associated with recognition events between carbohydrates and proteins [1,2]. Advances in chemical biology and biomedicine have benefitted from the emergence of small-molecule fluorescent probes [3,4] in combination with fluorescence spectroscopy or microscopy detection techniques [5,6,7,8,9,10] Encompassing these two research areas, several examples on the usefulness of fluorescently labeled carbohydrates in the investigation of biological processes have appeared in the literature [11,12,13,14]. A further refinement related to the aforementioned carbohydrate-protein interactions came with the realization that individual carbohydrate-ligands bind to a protein site weakly, and the high levels of recognition in biological events had to be associated to the existence of the so-called multivalent interactions [25].
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