Paving the Way for Practical Use of Sugar‐Binding Natural Products as Lectin Mimics in Glycobiological Research

Abstract

Figure 4. A) Complex-forming process of PRMswith aCa 2 + ion and Man. B) The calcium carboxylate model proposed in 1993, [9] in which two PRM molecules are bridged by aCa 2 + ion throught heir C18 carboxylate groups. C) Partial structure of aP RM-based Man chemosensord eveloped by Enomoto et al. [15]

Carbohydrate recognition using metal–ligand assemblies

“…4b) by the displacement of 19, increasing its fluorescence intensity. While all monosaccharides studied showed similar binding affinity, only fructose (7) and ribose (12) showed excellent fluorescence response with I/I 0 values of 6.5 and 6.2, respectively. Although this elegant design demonstrates the binding of weakly coordinating sugars to the free coordination sites of metal ions, the practical application of this design is limited due to poor selectivity.…”

“…The sugar-binding studies with the mononuclear Cu(II) species of 2-(( pyridine-2-ylmethyl)amino) ethan-1-ol 28b confirmed that the dinuclear Cu(II) binding site was crucial for achieving the selectivity. Interestingly, among structurally similar carbohydrates, 3 could differentiate D-mannose (4) from D-glucose ( 9) and D-galactose (8), and similarly D-ribose (12) from D-xylose (16), and D-arabinose (17), with a binding affinity about 1.5 orders of magnitude higher (Table 1). The monosaccharides, mannose and ribose, exhibit higher binding affinities with Cu(II) ions using cis,cis-triols at positions C-1, C-2 and C-3.…”

“…10 Binding between carbohydrate and lectin in water is primarily favoured by; (i) CH–π interactions between apolar –CH groups of the carbohydrate skeleton and the aromatic residues, and (ii) ion–dipole interactions between the carbohydrates and polar residues such as arginine, guanidine and aspartic acid including bound metal ions (particularly Ca 2+ ) of lectins. Inspired by the galactose chemoreceptor protein, 11 over the last three decades, synthetic chemists have designed and studied a variety of natural, 12 semisynthetic and artificial receptors 5,6,13–16 to distinguish different classes of carbohydrates in organic 14 and aqueous media. 15 Despite spectacular progress in carbohydrate recognition, selecting specific carbohydrates using simple building blocks remains scarce.…”

Leveraging Lucrative Lectins: An Explorative Review of the Biomedical Properties of Lectins

“…Pradimicin-A (PRM-A), an antifungal antibiotic, is among the first groups of "artificial lectins" that displays predominant binding towards HMGs on viral envelope. This is being considered as one of the promising drug candidates targeted against HIV-1/2 and Simian Immunodeficiency Viruses (SIVs) [85]. Another potent virus causing globally high levels of morbidity and mortality is the Severe Acute Respiratory Syndrome Coronavirus-2 (SARS-CoV2).…”

A Pradimicin-Based Staining Dye for Glycoprotein Detection

“…PRMs bind d -mannose (Man) in the presence of Ca 2+ and completely discriminate Man from its enantiomer ( l -mannose), epimers ( d -glucose, d -altrose, d -talose), amino derivatives ( d -mannosamine, N -acetyl- d -mannosamine), and other common monosaccharides ( d -galactose, N -acetyl- d -glucosamine, l -fucose, N -acetylneuraminic acid) . In addition, and quite significantly, PRMs have the capacity to bind biologically and pathologically important glycans that contain Man residues, such as N -linked glycans and fungal mannans. − While significant advances have been made in the design of sugar-binding small molecules, − such specific recognition of Man residues is yet to be achieved by the existing artificial molecules, thereby highlighting the great potential of PRMs for use as unique mimics of lectins. − …”