Utilize este identificador para referenciar este registo:
https://hdl.handle.net/1822/74755
Título: | Expanding the conformational landscape of minimalistic tripeptides by their O‑glycosylation |
Autor(es): | Brito, Alexandra Manuela Fernandes Dave, Dhwanit Lampel, Ayala Castro, Vânia Isabel Baptista Kroiss, Daniela Reis, R. L. Tuttle, Tell Ulijn, Rein V. Pires, R. A. Pashkuleva, I. |
Palavras-chave: | Aggregation CH-pi interactions GLYCOSYLATION Reductionist approach Self-assembly |
Data: | Nov-2021 |
Editora: | American Chemical Society |
Revista: | Journal of the American Chemical Society |
Citação: | Brito A., Dave D., Lampel A., Castro V. I. B., Kroiss D., Reis R. L., Tuttle T., Ulijn R. V., Pires R. A., Pashkuleva I. Expanding the conformational landscape of minimalistic tripeptides by their O‑glycosylation, Journal of the American Chemical Society, pp. in press, doi:10.1021/jacs.1c07592, 2021 |
Resumo(s): | 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 Ï 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. |
Tipo: | Artigo |
URI: | https://hdl.handle.net/1822/74755 |
DOI: | 10.1021/jacs.1c07592 |
ISSN: | 1520-5126 |
Versão da editora: | https://pubs.acs.org/doi/10.1021/jacs.1c07592 |
Arbitragem científica: | yes |
Acesso: | Acesso aberto |
Aparece nas coleções: | 3B’s - Artigos em revistas/Papers in scientific journals |
Ficheiros deste registo:
Ficheiro | Descrição | Tamanho | Formato | |
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20623-jacs1c07592.pdf | 8,26 MB | Adobe PDF | Ver/Abrir |