Microcantilever based on flavoenzyme monoamine oxidase (MAO) as a bioprobe

Microcantilevers (mcls) are cost-effective and highly sensitive devices for biodetection. adsorption of specific analytes on the microcantilever surface causes the bending of mcl through changing of the surface characteristics. these new bioprobes designed in a way that one side of the microcantilever surface is coated with a selective receptor that absorbs particular molecules. after surface absorption of target, the microcantilever deflects under nano – newton forces and results in microcantilever bending. in the following work, we have proposed a modifed microcantilever through immobilization of monoamine oxidase (mao) as a flavin–adenosine-dinucleotide (fad)-containing enzyme. this enzyme catalyzes the oxidative deamination of amine groups, so interaction between compounds with amine functional group and enzyme is based on biodetection with monoamine oxidase modified microcantilever. in the present study, mao was immobilized on the microcantilever surface through a cross linker to a monolayer on the gold surface. following, the kynuramine solution was used as substrate. the comparative results showed that the enzyme is activated in immobilized state in order to oxidize amine groups and is inhibited in the presence of methamphethamine as an enzyme inhibitor. since all processes are performing at room temperature, therefore the design of bioprobe based on modified microcantilever would be highly significant forbiodetection.