Sugars play crucial roles in biological processes, but their structural complexity and affinity for water make them challenging targets for selective binding. Even nature’s own carbohydrate-recognizing proteins, lectins, often struggle to bind simple sugars effectively, with binding affinities typically below 10³ M⁻¹. Our researcher invented a synthetic lectin that addresses this challenge. The receptor has a flexible and adaptive binding pocket that selectively binds glucose through reversible noncovalent interactions such as hydrogen bonding and hydrophobic effect. With an impressive binding affinity of 3000 M⁻¹ for glucose in water, our molecule surpasses the performance of natural lectins like concanavalin A by more than five times. X-ray crystallography reveals that each glucose molecule forms eight hydrogen bonds within the binding pocket, ensuring a strong, specific, and reliable interaction—a significant advancement for carbohydrate recognition.
In addition to its superior binding performance, our synthetic lectin is designed for efficient, scalable production. Using dynamic imine chemistry followed by a simple Pinnick oxidation, we’ve streamlined the synthesis process to be cost-effective and suitable for large-scale manufacturing. This receptor has immediate applications as a sensitive glucose sensor in water, PBS buffer, and other biological solutions, with further potential for detecting a range of sugars and carbohydrate-based biomarkers. We are seeking investors to help bring this innovative technology to market, offering a unique opportunity to lead advancements in biotechnology, diagnostics, and healthcare.
Structural formula of BPAT2+•2Cl– and single crystal structure complexed with glucose.