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• W2974488688 abstract "Mini protein is used as an alternative bioreceptor to native enzyme, which is costly andless stable. Mini protein that mimics enzyme may be utilized as the bioreceptor for thedetermination of metabolite in biological fluids. In this study, a novel uric acidbiosensor of mini protein immobilized onto screen printed carbon electrodes (SPEs)was developed for uric acid detection to replace conventional method. Uricase is alarge tetrameric protein carrying two active sites in each pair of dimer. This generatesan interest for a mini protein to function as bioreceptor that may replace the largenative enzymes. Five mini proteins comprising 20, 40, 60, 80 and 100 amino acidswere designed based on the conserved active site residues within the same dimer, usingthe 2yzb template. Utilizing Yet Another Scientific Artificial Reality Application(YASARA) software, four target structures were predicted for each mini protein model,by multistep process of homology modeling. Then the stereochemical quality of thestructure model was verified by PROCHECK and ERRAT programs. The bestevaluated structures (model 3 of mp20, model 2 of mp40, model 3 of mp60, model 3 ofmp80 and model 2 of mp100) were simulated with molecular dynamics (MD)simulations using YASARA, to study protein stability and folding. Five mini proteinswith the highest binding energy (enzyme-substrate complex) from docking werechosen in MD simulation analysis (mini protein and the substrate). The results alsoproved that the present of substrate in the protein structure helped to improve proteinfolding. Five recombinants of mini proteins (mp20, mp40, mp60, mp80 and mp100)were constructed in pET32a vector and all of them were successfully expressed into E.coli Bl21 (DE3). The smallest mini protein with 20 amino acids (mp20) was chosen forHis-tag affinity purification. The purified mp20 showed no activity in uricase assay.Subsequently, the approach was to look for binding affinity of mini protein andsubstrate (uric acid) via Isothermal titration calorimetry (ITC) and circular dichroism(CD) spectra. The ITC and CD results had proven that there was binding interactionbetween uric acid and the mini protein structure. A disposable uric acid biosensor onmodified gold nanowires screen printed carbon electrode (SPEs) was fabricated. Theworking surface of the SPEs electrode was modified by gold nanowires deposited onthe surface, followed by self-assembly of L-cysteine and glutaraldehyde. The miniprotein immobilized SPEs was studied and compared to uricase immobilized SPEs as positive control. The electrocatalytic oxidation of uric acid was examined using cyclicvoltammetry (CV) of a range between -1.0 and 1.0 V, at working potential 0.4 V (50mVs-1 scan rate). The sensor demonstrated that by using mini protein as thebioreceptor, the nanowire biosensor exhibited similar stability, sensitivity, selectivity,good reproducibility and repeatability for uric acid determination, with a linear rangefrom 0.01 mM to 1.0 mM and a detection limit of 0.1 mM as compared to control(uricase as the bioreceptor). Interestingly, the mini protein immobilized SPEs hadstrong affinity for uric acid compared to uricase immobilized SPEs with small value ofthe apparent Michaelis-Menten Constant (KMapp). Besides, The mini proteinimmobilized SPEs had similar performance as compared to commercial uric acidbiosensor in the market. In conclusion, the developed mini protein immobilized SPEscan be considered as a useful tool to replace conventional method in uric aciddetection." @default.
• W2974488688 created "2019-09-26" @default.
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• W2974488688 date "2017-05-01" @default.
• W2974488688 modified "2023-09-23" @default.
• W2974488688 title "Design of mini protein that mimics uricase in the preliminary development of nanowire-based uric acid biosensor" @default.
• W2974488688 hasPublicationYear "2017" @default.
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