Simulated revelation of the adsorption behaviours of acetylcholinesterase on charged self-assembled monolayers

Abstract

Electrostatically driven enzyme orientation leads to different enzyme activities and electron transfer rates on different charged surfaces.

Molecular understanding of acetylcholinesterase adsorption on functionalized carbon nanotubes for enzymatic biosensors

“…Although TcAChE has the same charge characteristics as the COOH–CNT surface with a net charge of −7 e , it can still be stably adsorbed on the surface, which indicates that the regulation of the electric dipole and the uneven distribution of electrostatic potential are the decisive factors of protein adsorption on the charge-like surface, rather than the charged property of the whole protein. This is consistent with the finding in our previous studies, 54,56,58 i.e. , the adsorption orientation of the protein on the charged surface is simultaneously regulated by the electric dipole and the distribution of the electrostatic potential.…”

“…Previous studies have shown that due to the strong electrostatic interaction between enzymes and surfaces, the adsorption orientation of enzymes on the charged surfaces could be controlled. 54–58 Yu et al 40 developed a new type of OP biosensor with high sensitivity by effectively immobilizing acetylcholinesterase on the surface of amino-functionalized CNT (NH 2 –CNT). They found that the adsorption capacity of acetylcholinesterase on the NH 2 –CNT was higher than those on pristine CNT, OH–CNT and COOH–CNT; the optimal current response was obtained on the NH 2 –CNT glassy carbon electrode.…”

Design of engineered surfaces for prospective detection of SARS-CoV-2 using quartz crystal microbalance-based techniques

“…Typically, adsorbed amount increase with an increase in surface hydrophobicity [23,24]. The protein adsorption is reported to be entropy driven and the conformations of the adsorbed protein molecules are found to depend on the surface chemistry [25,26], which plays a key role in the detection process. A recent study reported that acetylcholinesterase adsorbed in the 'end-on' orientation on the positively charged surface and in the 'back-on' orientation on the negatively charged surfaces and thus its catalytic activities were altered [26].…”

“…The protein adsorption is reported to be entropy driven and the conformations of the adsorbed protein molecules are found to depend on the surface chemistry [25,26], which plays a key role in the detection process. A recent study reported that acetylcholinesterase adsorbed in the 'end-on' orientation on the positively charged surface and in the 'back-on' orientation on the negatively charged surfaces and thus its catalytic activities were altered [26]. It suggested that functional groups present on a surface regulate the orientation of the adsorbed/attached protein and which in turn control the biocatalytic reaction.…”

CdTe QD-based inhibition and reactivation assay of acetylcholinesterase for the detection of organophosphorus pesticides

“…With high sensitivity and simplication, uorescence-based sensors have been widely applied as one of the most commonly used sensing candidates for environmental monitoring, 8 food safety 9 and quality control. 10 Quite recently, many optical [11][12][13] and electrochemical [14][15][16] methods/biosensors have been applied to determine pesticide residues in food samples. Various kinds of materials have been widely employed for the fabrication of a uorescence (FL) sensing platform, including uorescent dyes, 17 semiconductor nanomaterials, 18 metal nanomaterials, 19,20 carbon quantum dots (CQD), 21 and rare earth materials.…”