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Updated: Apr 17, 2026

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
Published on: January 20, 2022
Dissecting molecular aspects of cell interactions using glycodendrimersomes with programmable glycan presentation and
Shaodong Zhang1, Ralph-Olivier Moussodia, Claire Murzeau
1Roy & Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6323 (USA) http://percec02.chem.upenn.edu/
Abstract:
Glycodendrimersomes with programmable surface display of glycan, together with artificially engineered galectins, were used to understand the physiological significance of human lectins with homodimeric and tandem-repeat-type displays. The mode of topological surface presentation and the density of glycan affected vesicle aggregation mediated by multivalent carbohydrate-protein interactions. The cross-linking capacity of homodimeric lectins was enhanced by covalent connection of the two carbohydrate-binding sites. These findings highlight the value of glycodendrimersomes as versatile cell membrane mimetics, and assays provide diagnostic tools for protein functionality. This work also provides guidelines for the design of cell separators, bioactive matrices, bioeffectors, and other biomedical applications.
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