“Click” Saccharide/β-Lactam Hybrids for Lectin Inhibition

Hybrid glycopeptide β-lactam mimetics designed to bind lectins or carbohydrate recognition domains in selectins have been prepared according to a “shape-modulating linker” design. This approach was implemented using the azide−alkyne “click” cycloaddition reaction, and as shown by NMR/MD experiments,...

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Bibliographic Details
Published in:Organic letters 2008-06, Vol.10 (11), p.2227-2230
Main Authors: Palomo, Claudio, Aizpurua, Jesus M, Balentová, Eva, Azcune, Itxaso, Santos, J. Ignacio, Jiménez-Barbero, Jesús, Cañada, Javier, Miranda, José Ignacio
Format: Article
Language:English
Subjects:
beta-Lactams - chemistry
beta-Lactams - pharmacology
Biomimetic Materials - chemistry
Biomimetic Materials - pharmacology
Glycopeptides - chemistry
Glycopeptides - pharmacology
Lectins - antagonists & inhibitors
Lectins - chemistry
Plant Proteins - antagonists & inhibitors
Plant Proteins - chemistry
Protein Conformation
Ulex - chemistry
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Summary:Hybrid glycopeptide β-lactam mimetics designed to bind lectins or carbohydrate recognition domains in selectins have been prepared according to a “shape-modulating linker” design. This approach was implemented using the azide−alkyne “click” cycloaddition reaction, and as shown by NMR/MD experiments, binding of the resulting mimetics to Ulex Europaeus Lectin-1 (UEL-1) occurred after a “bent-to-extended” conformational change around a partially rotatable triazolylmethylene moiety.
ISSN:1523-7060
1523-7052
DOI:10.1021/ol8006259