H2N2V1, Main, Exploration, bibRecord, 000857

Novel 3,4-disubstituted-Neu5Ac2en derivatives as probes to investigate flexibility of the influenza virus sialidase 150-loop.

Identifieur interne : 000857 ( Main/Exploration ); précédent : 000856; suivant : 000858

Novel 3,4-disubstituted-Neu5Ac2en derivatives as probes to investigate flexibility of the influenza virus sialidase 150-loop.

Auteurs : Santosh Rudrawar [Australie] ; Jeffrey C. Dyason ; Andrea Maggioni ; Robin J. Thomson ; Mark Von Itzstein

Source :

Bioorganic & medicinal chemistry [ 1464-3391 ] ; 2013.

RBID : pubmed:23800724

Descripteurs français

KwdFr :
- Acide N-acétyl-neuraminique (), Acide N-acétyl-neuraminique (analogues et dérivés), Acide N-acétyl-neuraminique (métabolisme), Acides sialiques (), Liaison aux protéines, Orthomyxoviridae (enzymologie), Sialidase (), Sialidase (métabolisme), Sondes moléculaires, Structure secondaire des protéines.
MESH :
- analogues et dérivés : Acide N-acétyl-neuraminique.
- enzymologie : Orthomyxoviridae.
- métabolisme : Acide N-acétyl-neuraminique, Sialidase.
- Acide N-acétyl-neuraminique, Acides sialiques, Liaison aux protéines, Sialidase, Sondes moléculaires, Structure secondaire des protéines.

English descriptors

KwdEn :
- Molecular Probes, N-Acetylneuraminic Acid (analogs & derivatives), N-Acetylneuraminic Acid (chemistry), N-Acetylneuraminic Acid (metabolism), Neuraminidase (chemistry), Neuraminidase (metabolism), Orthomyxoviridae (enzymology), Protein Binding, Protein Structure, Secondary, Sialic Acids (chemistry).
MESH :
- chemical , analogs & derivatives : N-Acetylneuraminic Acid.
- chemical , chemistry : N-Acetylneuraminic Acid, Neuraminidase, Sialic Acids.
- chemical , metabolism : N-Acetylneuraminic Acid, Neuraminidase.
- chemical : Molecular Probes.
- enzymology : Orthomyxoviridae.
- Protein Binding, Protein Structure, Secondary.

Abstract

Novel 3,4-disubstituted-Neu5Ac2en derivatives have been synthesised to probe the open 150-loop conformation of influenza virus sialidases. Both equatorially and axially (epi) substituted C4 amino and guanidino 3-(p-tolyl)allyl-Neu5Ac2en derivatives were prepared, via the 4-epi-hydroxy derivative. The equatorially-substituted 4-amino derivative showed low micromolar inhibition of both group-1 (pdm09 H1N1) and group-2 (pdm57 H2N2) sialidases, and provides the first in vitro evidence that a group-2 sialidase may exhibit 150-loop flexibility.

DOI: 10.1016/j.bmc.2013.05.054
PubMed: 23800724

Affiliations:

Australie

Le document en format XML

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<term>N-Acetylneuraminic Acid (metabolism)</term>
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<front><div type="abstract" xml:lang="en">Novel 3,4-disubstituted-Neu5Ac2en derivatives have been synthesised to probe the open 150-loop conformation of influenza virus sialidases. Both equatorially and axially (epi) substituted C4 amino and guanidino 3-(p-tolyl)allyl-Neu5Ac2en derivatives were prepared, via the 4-epi-hydroxy derivative. The equatorially-substituted 4-amino derivative showed low micromolar inhibition of both group-1 (pdm09 H1N1) and group-2 (pdm57 H2N2) sialidases, and provides the first in vitro evidence that a group-2 sialidase may exhibit 150-loop flexibility. </div>
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Serveur d'exploration H2N2

Novel 3,4-disubstituted-Neu5Ac2en derivatives as probes to investigate flexibility of the influenza virus sialidase 150-loop.

Novel 3,4-disubstituted-Neu5Ac2en derivatives as probes to investigate flexibility of the influenza virus sialidase 150-loop.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

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