Glycopeptide Self-Assembly Modulated by Glycan Stereochemistry through Glycan–Aromatic Interactions
Changdong He, Shuang Wu, Dangliang Liu, Changbiao Chi, Weilin Zhang, Ming Ma, Luhua Lai, Suwei Dong
Abstract
shows that the glycopeptides with either α- or β-anomers exhibit contrary gelating abilities, when the glycan moieties contain axial hydroxyl groups. A high-resolution X-ray crystallographic structure of the β-galactose-containing gelator, along with other results from spectroscopic, microscopic, and rheological experiments, indicate an unusual carbohydrate-aromatic CH-π bonding that promotes glycopeptide self-assembly. These mechanistic findings, particularly evidence obtained at the angstrom scale, illuminate an unconventional role that carbohydrates can play in building supramolecules. Potential biomaterials exploiting the CH-π bond-based stabilization, as exemplified by an enzyme-resistant hydrogel, may thus be developed.