622832-88-6Relevant articles and documents
Glycopeptide self-assembly modulated by glycan stereochemistry through glycan-aromatic interactions
Dong, Suwei,He, Changdong,Wu, Shuang,Liu, Dangliang,Chi, Changbiao,Zhang, Weilin,Ma, Ming,Lai, Luhua
, p. 17015 - 17023 (2020)
Carbohydrates are often utilized to provide hydrophilicity and hydroxyl-based hydrogen bonds in self-assembling glycopeptides, affording versatile scaffolds with wide applicability in biomedical research. However, how stereochemistry of carbohydrates impacts the self-assembly process remains unclear. Here we have established a dimeric tyrosine-rich glycopeptide system for probing the corresponding hydrogelating behavior under the influence of site- and stereospecific glycosylations. Comparison of 18 glycoforms bearing monosaccharides at Tyr4 and Tyr4' 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 enzymeresistant hydrogel, may thus be developed.
S-2,4,6-Trimethoxybenzyl (Tmob): A novel cysteine protecting group for the N(α)-9-fluorenylmethoxycarbonyl (Fmoc) strategy of peptide synthesis
Munson,Garcia-Echeverria,Albericio,Barany
, p. 3013 - 3018 (2007/10/02)
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