Rational Design and Synthesis of Optimized Glycoclusters for
Multivalent Lectin-Carbohydrate Interactions: Influence of the
Linker Arm

J 2012

Rational Design and Synthesis of Optimized Glycoclusters for Multivalent Lectin-Carbohydrate Interactions: Influence of the Linker Arm

CECIONI, Samy; Jean-Pierre PRALY; Susan E MATTHEWS; Michaela WIMMEROVÁ; Anne IMBERTY et al.

Základní údaje

Originální název

Rational Design and Synthesis of Optimized Glycoclusters for Multivalent Lectin-Carbohydrate Interactions: Influence of the Linker Arm

Autoři

CECIONI, Samy; Jean-Pierre PRALY; Susan E MATTHEWS; Michaela WIMMEROVÁ; Anne IMBERTY a Sebastien VIDAL

Vydání

Chemistry - A European Journal, WEINHEIM, WILEY-VCH, 2012, 0947-6539

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Německo

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 5.831

Kód RIV

RIV/00216224:14740/12:00061938

Organizační jednotka

Středoevropský technologický institut

DOI

https://doi.org/10.1002/chem.201200010

UT WoS

000303497600019

Klíčová slova anglicky

carbohydrates; click chemistry; glycoclusters; lectin; multivalency

Štítky

ok, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 6. 4. 2013 18:15, Olga Křížová

Anotace

V originále

The design of multivalent glycoclusters requires the conjugation of biologically relevant carbohydrate epitopes functionalized with linker arms to multivalent core scaffolds. The multigram-scale syntheses of three structurally modified triethyleneglycol analogues that incorporate amide moiety(ies) and/or a phenyl ring offer convenient access to a series of carbohydrate probes with different water solubilities and rigidities. Evaluation of flexibility and determination of preferred conformations were performed by conformational analysis. Conjugation of the azido-functionalized carbohydrates with tetra-propargylated core scaffolds afforded a library of 18 tetravalent glycoclusters, in high yields, by CuI-catalyzed azidealkyne cycloaddition (CuAAC). The compounds were evaluated for their ability to bind to PA-IL (the LecA lectin from the opportunistic pathogen Pseudomonas aeruginosa). Biochemical evaluation through inhibition of hemagglutination assays (HIA), enzyme-linked lectin assays (ELLA), surface plasmon resonance (SPR), and isothermal titration microcalorimetry (ITC) revealed improved and unprecedented affinities for one of the monovalent probes (K-d=5.8 mu M) and also for a number of the tetravalent compounds that provide several new nanomolar ligands for this tetrameric lectin.

Návaznosti

ME08008, projekt VaV

Název: Návrh antibakteriálních a antivirových léků na bázi cukrů a glykomimetik

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Návrh antibakteriálních a antivirových léků na bázi cukrů a glykomimetik, Program výzkumu a vývoje KONTAKT (ME)

MSM0021622413, záměr

Název: Proteiny v metabolismu a při interakci organismů s prostředím

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Proteiny v metabolismu a při interakci organismů s prostředím

205872, interní kód MU

Název: Program developing interdisciplinary research POtential for the STudies of BIOMolecular INteractions (Akronym: POSTBIOMIN)

Investor: Evropská unie, Program developing interdisciplinary research POtential for the STudies of BIOMolecular INteractions, Kapacity

Přiložené soubory

2012_Chemistry_EJ.pdf

Požádat o autorskou verzi souboru

Citovat

CECIONI, Samy; Jean-Pierre PRALY; Susan E MATTHEWS; Michaela WIMMEROVÁ; Anne IMBERTY a Sebastien VIDAL. Rational Design and Synthesis of Optimized Glycoclusters for Multivalent Lectin-Carbohydrate Interactions: Influence of the Linker Arm. Chemistry - A European Journal. WEINHEIM: WILEY-VCH, 2012, roč. 18, č. 20, s. 6250-6263. ISSN 0947-6539. Dostupné z: https://doi.org/10.1002/chem.201200010.

@article{1073530,
   author = {Cecioni, Samy and Praly, JeanandPierre and Matthews, Susan E and Wimmerová, Michaela and Imberty, Anne and Vidal, Sebastien},
   article_location = {WEINHEIM},
   article_number = {20},
   doi = {https://doi.org/10.1002/chem.201200010},
   keywords = {carbohydrates; click chemistry; glycoclusters; lectin; multivalency},
   language = {eng},
   issn = {0947-6539},
   journal = {Chemistry - A European Journal},
   title = {Rational Design and Synthesis of Optimized Glycoclusters for Multivalent Lectin-Carbohydrate Interactions: Influence of the Linker Arm},
   url = {http://onlinelibrary.wiley.com/doi/10.1002/chem.201200010/suppinfo},
   volume = {18},
   year = {2012}
}

TY  - JOUR
ID  - 1073530
AU  - Cecioni, Samy - Praly, Jean-Pierre - Matthews, Susan E - Wimmerová, Michaela - Imberty, Anne - Vidal, Sebastien
PY  - 2012
TI  - Rational Design and Synthesis of Optimized Glycoclusters for Multivalent Lectin-Carbohydrate Interactions: Influence of the Linker Arm
JF  - Chemistry - A European Journal
VL  - 18
IS  - 20
SP  - 6250-6263
EP  - 6250-6263
PB  - WILEY-VCH
SN  - 09476539
KW  - carbohydrates
KW  - click chemistry
KW  - glycoclusters
KW  - lectin
KW  - multivalency
UR  - http://onlinelibrary.wiley.com/doi/10.1002/chem.201200010/suppinfo
L2  - http://onlinelibrary.wiley.com/doi/10.1002/chem.201200010/suppinfo
N2  - The design of multivalent glycoclusters requires the conjugation of biologically relevant carbohydrate epitopes functionalized with linker arms to multivalent core scaffolds. The multigram-scale syntheses of three structurally modified triethyleneglycol analogues that incorporate amide moiety(ies) and/or a phenyl ring offer convenient access to a series of carbohydrate probes with different water solubilities and rigidities. Evaluation of flexibility and determination of preferred conformations were performed by conformational analysis. Conjugation of the azido-functionalized carbohydrates with tetra-propargylated core scaffolds afforded a library of 18 tetravalent glycoclusters, in high yields, by CuI-catalyzed azidealkyne cycloaddition (CuAAC). The compounds were evaluated for their ability to bind to PA-IL (the LecA lectin from the opportunistic pathogen Pseudomonas aeruginosa). Biochemical evaluation through inhibition of hemagglutination assays (HIA), enzyme-linked lectin assays (ELLA), surface plasmon resonance (SPR), and isothermal titration microcalorimetry (ITC) revealed improved and unprecedented affinities for one of the monovalent probes (K-d=5.8 mu M) and also for a number of the tetravalent compounds that provide several new nanomolar ligands for this tetrameric lectin.
ER  -

CECIONI, Samy; Jean-Pierre PRALY; Susan E MATTHEWS; Michaela WIMMEROVÁ; Anne IMBERTY a Sebastien VIDAL. Rational Design and Synthesis of Optimized Glycoclusters for Multivalent Lectin-Carbohydrate Interactions: Influence of the Linker Arm. \textit{Chemistry - A European Journal}. WEINHEIM: WILEY-VCH, 2012, roč.~18, č.~20, s.~6250-6263. ISSN~0947-6539. Dostupné z: https://doi.org/10.1002/chem.201200010.

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