Fucosylated ubiquitin and orthogonally glycosylated mutant A28C: Conceptually new ligands for: Burkholderia ambifaria lectin (BambL)

Sakonwan Kuhaudomlarp; Linda Cerofolini; Sabrina Santarsia; Emilie Gillon; Silvia Fallarini; Grazia Lombardi; Maxime Denis; Stefano Giuntini; Carolina Valori; Marco Fragai; Anne Imberty; Alessandro Dondoni; Cristina Nativi

doi:10.1039/d0sc03741a

Fucosylated ubiquitin and orthogonally glycosylated mutant A28C: Conceptually new ligands for: Burkholderia ambifaria lectin (BambL)

Sakonwan Kuhaudomlarp, Linda Cerofolini, Sabrina Santarsia, Emilie Gillon, Silvia Fallarini, Grazia Lombardi, Maxime Denis, Stefano Giuntini, Carolina Valori, Marco Fragai, Anne Imberty, Alessandro Dondoni, Cristina Nativi

Dipartimento di Scienze del Farmaco

Risultato della ricerca: Contributo su rivista › Articolo in rivista › peer review

Abstract

Two orthogonal, metal free click reactions, enabled to glycosylate ubiquitin and its mutant A28C forming two protein scaffolds with high affinity for BambL, a lectin from the human pathogen Burkholderia ambifaria. A new fucoside analogue, with high affinity with BambL, firstly synthetized and co-crystallized with the protein target, provided the insights for sugar determinants grafting onto ubiquitin. Three ubiquitin-based glycosides were thus assembled. Fuc-Ub, presented several copies of the fucoside analogue, with proper geometry for multivalent effect; Rha-A28C, displayed one thio-rhamnose, known for its ability to tuning the immunological response; finally, Fuc-Rha-A28C, included both multiple fucoside analogs and the rhamnose residue. Fuc-Ub and Fuc-Rha-A28C ligands proved high affinity for BambL and unprecedented immune modulatory properties towards macrophages activation.

Lingua originale	Inglese
pagine (da-a)	12662-12670
Numero di pagine	9
Rivista	Chemical Science
Volume	11
Numero di pubblicazione	47
DOI	https://doi.org/10.1039/d0sc03741a
Stato di pubblicazione	Pubblicato - 21 dic 2020

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10.1039/d0sc03741a

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Kuhaudomlarp, S., Cerofolini, L., Santarsia, S., Gillon, E., Fallarini, S., Lombardi, G., Denis, M., Giuntini, S., Valori, C., Fragai, M., Imberty, A., Dondoni, A., & Nativi, C. (2020). Fucosylated ubiquitin and orthogonally glycosylated mutant A28C: Conceptually new ligands for: Burkholderia ambifaria lectin (BambL). Chemical Science, 11(47), 12662-12670. https://doi.org/10.1039/d0sc03741a

@article{bde95c50548043e494356a46371009eb,

title = "Fucosylated ubiquitin and orthogonally glycosylated mutant A28C: Conceptually new ligands for: Burkholderia ambifaria lectin (BambL)",

abstract = "Two orthogonal, metal free click reactions, enabled to glycosylate ubiquitin and its mutant A28C forming two protein scaffolds with high affinity for BambL, a lectin from the human pathogen Burkholderia ambifaria. A new fucoside analogue, with high affinity with BambL, firstly synthetized and co-crystallized with the protein target, provided the insights for sugar determinants grafting onto ubiquitin. Three ubiquitin-based glycosides were thus assembled. Fuc-Ub, presented several copies of the fucoside analogue, with proper geometry for multivalent effect; Rha-A28C, displayed one thio-rhamnose, known for its ability to tuning the immunological response; finally, Fuc-Rha-A28C, included both multiple fucoside analogs and the rhamnose residue. Fuc-Ub and Fuc-Rha-A28C ligands proved high affinity for BambL and unprecedented immune modulatory properties towards macrophages activation.",

author = "Sakonwan Kuhaudomlarp and Linda Cerofolini and Sabrina Santarsia and Emilie Gillon and Silvia Fallarini and Grazia Lombardi and Maxime Denis and Stefano Giuntini and Carolina Valori and Marco Fragai and Anne Imberty and Alessandro Dondoni and Cristina Nativi",

note = "Publisher Copyright: {\textcopyright} 2020 The Royal Society of Chemistry.",

year = "2020",

month = dec,

day = "21",

doi = "10.1039/d0sc03741a",

language = "English",

volume = "11",

pages = "12662--12670",

journal = "Chemical Science",

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publisher = "Royal Society of Chemistry",

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Kuhaudomlarp, S, Cerofolini, L, Santarsia, S, Gillon, E, Fallarini, S, Lombardi, G, Denis, M, Giuntini, S, Valori, C, Fragai, M, Imberty, A, Dondoni, A & Nativi, C 2020, 'Fucosylated ubiquitin and orthogonally glycosylated mutant A28C: Conceptually new ligands for: Burkholderia ambifaria lectin (BambL)', Chemical Science, vol. 11, n. 47, pagg. 12662-12670. https://doi.org/10.1039/d0sc03741a

TY - JOUR

T1 - Fucosylated ubiquitin and orthogonally glycosylated mutant A28C

T2 - Conceptually new ligands for: Burkholderia ambifaria lectin (BambL)

AU - Kuhaudomlarp, Sakonwan

AU - Cerofolini, Linda

AU - Santarsia, Sabrina

AU - Gillon, Emilie

AU - Fallarini, Silvia

AU - Lombardi, Grazia

AU - Denis, Maxime

AU - Giuntini, Stefano

AU - Valori, Carolina

AU - Fragai, Marco

AU - Imberty, Anne

AU - Dondoni, Alessandro

AU - Nativi, Cristina

PY - 2020/12/21

Y1 - 2020/12/21

N2 - Two orthogonal, metal free click reactions, enabled to glycosylate ubiquitin and its mutant A28C forming two protein scaffolds with high affinity for BambL, a lectin from the human pathogen Burkholderia ambifaria. A new fucoside analogue, with high affinity with BambL, firstly synthetized and co-crystallized with the protein target, provided the insights for sugar determinants grafting onto ubiquitin. Three ubiquitin-based glycosides were thus assembled. Fuc-Ub, presented several copies of the fucoside analogue, with proper geometry for multivalent effect; Rha-A28C, displayed one thio-rhamnose, known for its ability to tuning the immunological response; finally, Fuc-Rha-A28C, included both multiple fucoside analogs and the rhamnose residue. Fuc-Ub and Fuc-Rha-A28C ligands proved high affinity for BambL and unprecedented immune modulatory properties towards macrophages activation.

AB - Two orthogonal, metal free click reactions, enabled to glycosylate ubiquitin and its mutant A28C forming two protein scaffolds with high affinity for BambL, a lectin from the human pathogen Burkholderia ambifaria. A new fucoside analogue, with high affinity with BambL, firstly synthetized and co-crystallized with the protein target, provided the insights for sugar determinants grafting onto ubiquitin. Three ubiquitin-based glycosides were thus assembled. Fuc-Ub, presented several copies of the fucoside analogue, with proper geometry for multivalent effect; Rha-A28C, displayed one thio-rhamnose, known for its ability to tuning the immunological response; finally, Fuc-Rha-A28C, included both multiple fucoside analogs and the rhamnose residue. Fuc-Ub and Fuc-Rha-A28C ligands proved high affinity for BambL and unprecedented immune modulatory properties towards macrophages activation.

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U2 - 10.1039/d0sc03741a

DO - 10.1039/d0sc03741a

M3 - Article

SN - 2041-6520

VL - 11

SP - 12662

EP - 12670

JO - Chemical Science

JF - Chemical Science

IS - 47

ER -

Fucosylated ubiquitin and orthogonally glycosylated mutant A28C: Conceptually new ligands for: Burkholderia ambifaria lectin (BambL)

Abstract

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