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

Department of Life Science, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 J2-10, Nagatsutacho, Midoriku, Yokohama 226-8501, Japan.
Bioorganic & Medicinal Chemistry Letters (Impact Factor: 2.34). 10/2007; 17(18):5274-8. DOI: 10.1016/j.bmcl.2006.12.075
Source: PubMed

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.

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