To identify molecular targets that interact with zosteric acid, a small-scale affinity purification of proteins from E. coli extracts on immobilized zosteric acid moieties was performed. According to the biological screening of the small library of molecules, p-aminocinnamic acid was selected for its covalent coupling to the affinity support. Functionalization of the solid support was successfully demonstrated by fluorescence analysis. The protein pull-down revealed that one protein bound to cinnamate coupled matrix. The identification of this protein is still in progress.

Antibiofilm activity of selected natural compounds / C. Cattò. ((Intervento presentato al 9. convegno Workshop. Doctorate in Chemistry, Biochemistry and Ecology of Plant Protection Products and Xenobiotics tenutosi a Milano nel 2014.

Antibiofilm activity of selected natural compounds

C. Cattò
Primo
2014

Abstract

To identify molecular targets that interact with zosteric acid, a small-scale affinity purification of proteins from E. coli extracts on immobilized zosteric acid moieties was performed. According to the biological screening of the small library of molecules, p-aminocinnamic acid was selected for its covalent coupling to the affinity support. Functionalization of the solid support was successfully demonstrated by fluorescence analysis. The protein pull-down revealed that one protein bound to cinnamate coupled matrix. The identification of this protein is still in progress.
gen-2014
Settore BIO/10 - Biochimica
Settore AGR/16 - Microbiologia Agraria
Antibiofilm activity of selected natural compounds / C. Cattò. ((Intervento presentato al 9. convegno Workshop. Doctorate in Chemistry, Biochemistry and Ecology of Plant Protection Products and Xenobiotics tenutosi a Milano nel 2014.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/232078
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