Pentamer is the minimum structure for oligomannosylpeptoids to bind to concanavalin A

ELLA disclosed the smallest oligomannosylpeptoid recognized by ConA. Enzyme-linked lectin assay (ELLA) was performed for oligomannosylpeptoids, which were immobilized on microtiter plates through a streptavidin–biotin interaction. The other immobilization methods, a hydrophobic adsorption and a cova...

Full description

Saved in:
Bibliographic Details
Published in:Bioorganic & medicinal chemistry letters 2007-09, Vol.17 (18), p.5274-5278
Main Authors: Yuasa, Hideya, Honma, Hiroyuki, Hashimoto, Hironobu, Tsunooka, Miyuki, Kojima-Aikawa, Kyoko
Format: Article
Language:English
Subjects:
Biological and medical sciences
Concanavalin A
Concanavalin A - metabolism
ELLA
Mannose - metabolism
Mannosylpeptoids
Medical sciences
Miscellaneous
Molecular Structure
Oligosaccharide mimics
Peptoids - chemistry
Peptoids - metabolism
Pharmacology. Drug treatments
Protein Binding
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:ELLA disclosed the smallest oligomannosylpeptoid recognized by ConA. Enzyme-linked lectin assay (ELLA) was performed for oligomannosylpeptoids, which were immobilized on microtiter plates through a streptavidin–biotin interaction. The other immobilization methods, a hydrophobic adsorption and a covalent attachment, were found inapplicable to the oligomannosylpeptoids. Penta- and hexamannosylpeptoids with a shorter or longer spacer were found to be significantly recognized by concanavalinA (ConA), while the smaller peptoids showed no bindings. A proportional relationship between the amount of bound ConA and the peptoid density on the microtiter plate was observed, indicating the absence of both cluster and overdense effects that would assist or inhibit the binding increasingly with the ligand density.
ISSN:0960-894X
1464-3405
DOI:10.1016/j.bmcl.2006.12.075