Multivalent Effect in Glycosidase Inhibition: The End of the Beginning.
biological activities
carbohydrates
click chemistry
cluster compounds
inhibitors
Journal
Chemical record (New York, N.Y.)
ISSN: 1528-0691
Titre abrégé: Chem Rec
Pays: United States
ID NLM: 101085550
Informations de publication
Date de publication:
Jan 2020
Jan 2020
Historique:
received:
23
01
2019
revised:
15
03
2019
pubmed:
18
4
2019
medline:
18
2
2020
entrez:
18
4
2019
Statut:
ppublish
Résumé
Glycosidases are ubiquitous enzymes involved in a diversity of key biological processes such as energy uptake or cell wall degradation. The design of specific glycosidase inhibitors has been therefore the subject of intense research efforts in academia and pharmaceutical industry. However, until recently, the study of the impact of multivalency on glycosidase inhibition was almost completely neglected. The following account will review our ten year journey on the design of multivalent glycomimetics within our research group, from the discovery of the first strong multivalent effect in glycosidase inhibition to the high-resolution crystal structures of Jack bean α-mannosidase in complex with the multimeric inhibitor displaying the largest binding enhancements reported so far.
Identifiants
pubmed: 30993894
doi: 10.1002/tcr.201900004
doi:
Substances chimiques
Enzyme Inhibitors
0
Glycoside Hydrolases
EC 3.2.1.-
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
10-22Subventions
Organisme : Universitaire de France (IUF), the CNRS, the University of Strasbourg, the Agence Nationale de la Recherche
ID : 11-BS07-003-02
Informations de copyright
© 2019 The Chemical Society of Japan & Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.
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