Expanding the conformational landscape of minimalistic tripeptides by their O‑glycosylation

last updated: 2022-01-04
ProjectCardioHeal :: publications list
TitleExpanding the conformational landscape of minimalistic tripeptides by their O‑glycosylation
Publication TypePapers in Scientific Journals
Year of Publication2021
AuthorsBrito A., Dave D., Lampel A., Castro V. I. B., Kroiss D., Reis R. L., Tuttle T., Ulijn R. V., Pires R. A., and Pashkuleva I.

We report on the supramolecular self-assembly of tripeptides and their O-glycosylated analogues, in which the carbohydrate moiety is coupled to a central serine or threonine flanked by phenylalanine residues. The substitution of serine with threonine introduces differential side-chain interactions, which results in the formation of aggregates with different morphology. O-glycosylation decreases the aggregation propensity because of rebalancing of the π interactions. The glycopeptides form aggregates with reduced stiffness but increased thermal stability. Our results demonstrate that the designed minimalistic glycopeptides retain critical functional features of glycoproteins and therefore are promising tools for elucidation of molecular mechanisms involved in the glycoprotein interactome. They can also serve as an inspiration for the design of functional glycopeptide-based biomaterials.

JournalJournal of the American Chemical Society
Pagination19703 - 19710
Date Published2021-11-19
PublisherAmerican Chemical Society
Keywordsaggregation, CH-pi interactions, GLYCOSYLATION, reductionist approach, self-assembly
RightsembargoedAccess (2 Years)
Peer reviewedyes

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