7C0N

Crystal structure of a self-assembling galactosylated peptide homodimer

Summary for 7C0N

• Entry DOI: 10.2210/pdb7c0n/pdb
• Descriptor: Self-assembling galactosylated tyrosine-rich peptide, beta-D-galactopyranose, SULFATE ION, ... (4 entities in total)
• Functional Keywords: self-assembling glycopeptide, tyrosine-rich peptide, o-glycan modification., de novo protein
• Biological source: synthetic construct
• Total number of polymer chains: 2
• Total formula weight: 2004.08

Authors

He, C.,Wu, S.,Chi, C.,Zhang, W.,Ma, M.,Lai, L.,Dong, S. (deposition date: 2020-05-01, release date: 2020-10-07, Last modification date: 2024-10-23)

Primary citation

He, C.,Wu, S.,Liu, D.,Chi, C.,Zhang, W.,Ma, M.,Lai, L.,Dong, S.
Glycopeptide Self-Assembly Modulated by Glycan Stereochemistry through Glycan-Aromatic Interactions.
J.Am.Chem.Soc., 142:17015-17023, 2020

PubMed Abstract: 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 Tyr and Tyr 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.

PubMed: 32946227
DOI: 10.1021/jacs.0c06360

Experimental method

X-RAY DIFFRACTION (1.552 Å)