Utilize este identificador para referenciar este registo:
https://hdl.handle.net/1822/74755
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Campo DC | Valor | Idioma |
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dc.contributor.author | Brito, Alexandra Manuela Fernandes | por |
dc.contributor.author | Dave, Dhwanit | por |
dc.contributor.author | Lampel, Ayala | por |
dc.contributor.author | Castro, Vânia Isabel Baptista | por |
dc.contributor.author | Kroiss, Daniela | por |
dc.contributor.author | Reis, R. L. | por |
dc.contributor.author | Tuttle, Tell | por |
dc.contributor.author | Ulijn, Rein V. | por |
dc.contributor.author | Pires, R. A. | por |
dc.contributor.author | Pashkuleva, I. | por |
dc.date.accessioned | 2021-11-22T13:24:20Z | - |
dc.date.available | 2023-12-01T07:00:28Z | - |
dc.date.issued | 2021-11 | - |
dc.date.submitted | 2021-11 | - |
dc.identifier.citation | 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 | por |
dc.identifier.issn | 1520-5126 | por |
dc.identifier.uri | https://hdl.handle.net/1822/74755 | - |
dc.description.abstract | 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. | por |
dc.description.sponsorship | We acknowledge the EU’s H2020 program (Forecast 668983) and the Portuguese FCT (BD/113794/2015; PTDC/BTMMAT/ 28327/2017 CARDIOHEAL; M-ERA-NET2/0001/ 2016 INCIPIT) for the financial support. Part of this research was supported by National Science Foundation (NSF) grant CHE-1808143 and a grant of computer time from the City University of New York High Performance Computing Center under NSF grants CNS-0855217, CNS-0958379, and ACI- 1126113. D.D. thanks Maithreyi Ramakrishnan for provision of a dihedral analysis script and Mateusz Marianski for discussions. | por |
dc.language.iso | eng | por |
dc.publisher | American Chemical Society | por |
dc.relation | info:eu-repo/grantAgreement/FCT/POR_NORTE/PD%2FBD%2F113794%2F2015/PT | por |
dc.relation | info:eu-repo/grantAgreement/FCT/9471 - RIDTI/PTDC%2FBTM-MAT%2F28327%2F2017/PT | por |
dc.relation | info:eu-repo/grantAgreement/EC/H2020/668983/EU | - |
dc.rights | openAccess | por |
dc.subject | Aggregation | por |
dc.subject | CH-pi interactions | por |
dc.subject | GLYCOSYLATION | por |
dc.subject | Reductionist approach | por |
dc.subject | Self-assembly | por |
dc.title | Expanding the conformational landscape of minimalistic tripeptides by their O‑glycosylation | por |
dc.type | article | - |
dc.peerreviewed | yes | por |
dc.relation.publisherversion | https://pubs.acs.org/doi/10.1021/jacs.1c07592 | por |
dc.comments | http://3bs.uminho.pt/node/20623 | por |
oaire.citationStartPage | 19703 | por |
oaire.citationEndPage | 19710 | por |
oaire.citationIssue | 47 | por |
oaire.citationVolume | 143 | por |
dc.date.updated | 2021-11-22T10:02:32Z | - |
dc.identifier.doi | 10.1021/jacs.1c07592 | por |
dc.identifier.pmid | 34797059 | por |
dc.subject.wos | Science & Technology | por |
sdum.journal | Journal of the American Chemical Society | por |
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 |