Synthetic Carbohydrate Receptors (SCRs) similarities with abamectin gamma-aminobutyric acid (GABA) glutamate-gated chloride channels

Synthetic Carbohydrate Receptors (SCRs) and abamectin-targeted channels (such as GABA and GluCl channels) share a fundamental biological similarity: they both utilize multivalent, non-covalent interactions to selectively recognize and bind to conserved glycan (sugar) structures.

How These Systems CompareWhile SCRs act as prophylactic antivirals and abamectin functions as a neurotoxic pesticide, their underlying biomolecular mechanisms are closely linked:

Targeting Conserved Sugars: SCRs are small-molecule tetrapodal structures explicitly designed to bind highly conserved envelope virus N-glycans. Similarly, invertebrate GABA and glutamate-gated chloride channels (GluCls) contain carbohydrate-binding motifs and are regulated by glycan-rich environments at synaptic terminals.

Mechanism of Action:SCRs: Bind to viral N-glycans, physically block the virus's ability to attach to host cell membranes, and stall membrane fusion.

Abamectin: Binds to allosteric sites on GluCls and GABA receptors, locking these chloride channels open. This causes an influx of chloride ions, which hyperpolarizes the nerve cell, resulting in permanent paralysis.

Structural Flexibility: Both systems avoid purely rigid binding. Natural sugar-binding proteins and SCRs both utilize flexibility and cooperative interactions to adjust their shapes to complex sugar topographies. Similarly, invertebrate GABA and GluCl receptors are heteromultimers that rely on structural subunit variations and spatial organization to modulate drug sensitivity.