Title of article
Pentamer is the minimum structure for oligomannosylpeptoids to bind to concanavalin A
Author/Authors
Hideya Yuasa، نويسنده , , Hiroyuki Honma، نويسنده , , Hironobu Hashimoto، نويسنده , , Miyuki Tsunooka، نويسنده , , Kyoko Kojima-Aikawa، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2007
Pages
5
From page
5274
To page
5278
Abstract
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.
Keywords
Mannosylpeptoids , Oligosaccharide mimics , concanavalin A , ELLA
Journal title
Bioorganic & Medicinal Chemistry Letters
Serial Year
2007
Journal title
Bioorganic & Medicinal Chemistry Letters
Record number
798597
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