Investigation of the Binding Affinity of a Broad Array of
L-Fucosides with Six Fucose-Specific Lectins of Bacterial and
Fungal Origin

J 2019

Investigation of the Binding Affinity of a Broad Array of L-Fucosides with Six Fucose-Specific Lectins of Bacterial and Fungal Origin

THAI LE, Son; Lenka MALINOVSKÁ; Michaela VAŠKOVÁ; Erika MEZO; Viktor KELEMEN et. al.

Základní údaje

Originální název

Investigation of the Binding Affinity of a Broad Array of L-Fucosides with Six Fucose-Specific Lectins of Bacterial and Fungal Origin

Autoři

THAI LE, Son; Lenka MALINOVSKÁ ; Michaela VAŠKOVÁ; Erika MEZO; Viktor KELEMEN; Anikó BORBÁS; Petr HODEK; Michaela WIMMEROVÁ a Magdolna CSÁVÁS

Vydání

Molecules, Mayer und Muller, 2019, 1420-3049

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10400 1.4 Chemical sciences

Stát vydavatele

Švýcarsko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 3.267

Kód RIV

RIV/00216224:14740/19:00107484

Organizační jednotka

Středoevropský technologický institut

DOI

https://doi.org/10.3390/molecules24122262

UT WoS

000473816900068

EID Scopus

2-s2.0-85068492657

Klíčová slova anglicky

l-fucosides; multivalency; lectins; glycoclusters; hemagglutination; cystic fibrosis

Štítky

CF BIC, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 27. 10. 2024 15:05, Ing. Martina Blahová

Anotace

V originále

Series of multivalent alpha-l-fucoside containing glycoclusters and variously decorated l-fucosides were synthesized to find potential inhibitors of fucose-specific lectins and study the structure-binding affinity relationships. Tri- and tetravalent fucoclusters were built using copper-mediated azide-alkyne click chemistry. Series of fucoside monomers and dimers were synthesized using various methods, namely glycosylation, an azide-alkyne click reaction, photoinduced thiol-en addition, and sulfation. The interactions between compounds with six fucolectins of bacterial or fungal origin were tested using a hemagglutination inhibition assay. As a result, a tetravalent, aplha-l-fucose presenting glycocluster showed to be a ligand that was orders of magnitude better than a simple monosaccharide for tested lectins in most cases, which can nominate it as a universal ligand for studied lectins. This compound was also able to inhibit the adhesion of Pseudomonas aeruginosa cells to human epithelial bronchial cells. A trivalent fucocluster with a protected amine functional group also seems to be a promising candidate for designing glycoconjugates and chimeras.

Návaznosti

GA15-17572S, projekt VaV

Název: Glykoklastry kalix[4]aren/C-oligosacharidy pro studium selektivity interakcí s lektiny

Investor: Grantová agentura ČR, Glykoklastry kalix[4]aren/C-oligosacharidy pro studium selektivity interakcí s lektiny

90043, velká výzkumná infrastruktura

Název: CIISB

Citovat

THAI LE, Son; Lenka MALINOVSKÁ; Michaela VAŠKOVÁ; Erika MEZO; Viktor KELEMEN; Anikó BORBÁS; Petr HODEK; Michaela WIMMEROVÁ a Magdolna CSÁVÁS. Investigation of the Binding Affinity of a Broad Array of L-Fucosides with Six Fucose-Specific Lectins of Bacterial and Fungal Origin. Molecules. Mayer und Muller, 2019, roč. 24, č. 12, s. 1-17. ISSN 1420-3049. Dostupné z: https://doi.org/10.3390/molecules24122262.

@article{1543778,
   author = {Thai Le, Son and Malinovská, Lenka and Vašková, Michaela and Mezo, Erika and Kelemen, Viktor and Borbás, Anikó and Hodek, Petr and Wimmerová, Michaela and Csávás, Magdolna},
   article_number = {12},
   doi = {https://doi.org/10.3390/molecules24122262},
   keywords = {l-fucosides; multivalency; lectins; glycoclusters; hemagglutination; cystic fibrosis},
   language = {eng},
   issn = {1420-3049},
   journal = {Molecules},
   title = {Investigation of the Binding Affinity of a Broad Array of L-Fucosides with Six Fucose-Specific Lectins of Bacterial and Fungal Origin},
   url = {https://www.mdpi.com/1420-3049/24/12/2262},
   volume = {24},
   year = {2019}
}

TY  - JOUR
ID  - 1543778
AU  - Thai Le, Son - Malinovská, Lenka - Vašková, Michaela - Mezo, Erika - Kelemen, Viktor - Borbás, Anikó - Hodek, Petr - Wimmerová, Michaela - Csávás, Magdolna
PY  - 2019
TI  - Investigation of the Binding Affinity of a Broad Array of L-Fucosides with Six Fucose-Specific Lectins of Bacterial and Fungal Origin
JF  - Molecules
VL  - 24
IS  - 12
SP  - 1-17
EP  - 1-17
PB  - Mayer und Muller
SN  - 14203049
KW  - l-fucosides
KW  - multivalency
KW  - lectins
KW  - glycoclusters
KW  - hemagglutination
KW  - cystic fibrosis
UR  - https://www.mdpi.com/1420-3049/24/12/2262
L2  - https://www.mdpi.com/1420-3049/24/12/2262
N2  - Series of multivalent alpha-l-fucoside containing glycoclusters and variously decorated l-fucosides were synthesized to find potential inhibitors of fucose-specific lectins and study the structure-binding affinity relationships. Tri- and tetravalent fucoclusters were built using copper-mediated azide-alkyne click chemistry. Series of fucoside monomers and dimers were synthesized using various methods, namely glycosylation, an azide-alkyne click reaction, photoinduced thiol-en addition, and sulfation. The interactions between compounds with six fucolectins of bacterial or fungal origin were tested using a hemagglutination inhibition assay. As a result, a tetravalent, aplha-l-fucose presenting glycocluster showed to be a ligand that was orders of magnitude better than a simple monosaccharide for tested lectins in most cases, which can nominate it as a universal ligand for studied lectins. This compound was also able to inhibit the adhesion of Pseudomonas aeruginosa cells to human epithelial bronchial cells. A trivalent fucocluster with a protected amine functional group also seems to be a promising candidate for designing glycoconjugates and chimeras.
ER  -

THAI LE, Son; Lenka MALINOVSKÁ; Michaela VAŠKOVÁ; Erika MEZO; Viktor KELEMEN; Anikó BORBÁS; Petr HODEK; Michaela WIMMEROVÁ a Magdolna CSÁVÁS. Investigation of the Binding Affinity of a Broad Array of L-Fucosides with Six Fucose-Specific Lectins of Bacterial and Fungal Origin. \textit{Molecules}. Mayer und Muller, 2019, roč.~24, č.~12, s.~1-17. ISSN~1420-3049. Dostupné z: https://doi.org/10.3390/molecules24122262.

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