Literature DB >> 17689075

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

Hideya Yuasa1, Hiroyuki Honma, Hironobu Hashimoto, Miyuki Tsunooka, Kyoko Kojima-Aikawa.   

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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Year:  2006        PMID: 17689075     DOI: 10.1016/j.bmcl.2006.12.075

Source DB:  PubMed          Journal:  Bioorg Med Chem Lett        ISSN: 0960-894X            Impact factor:   2.823


  6 in total

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Journal:  Org Biomol Chem       Date:  2009-02-11       Impact factor: 3.876

Review 4.  Solid-phase synthesis of N-substituted glycine oligomers (alpha-peptoids) and derivatives.

Authors:  Adrian S Culf; Rodney J Ouellette
Journal:  Molecules       Date:  2010-08-04       Impact factor: 4.411

5.  Dietary restriction abrogates antibody production induced by a DNA vaccine encoding the mycobacterial 65 kDa heat shock protein.

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Review 6.  Targeting the androgen receptor with steroid conjugates.

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  6 in total

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