Commonly, in the artificial enzyme-involved signal amplification approach, the catalytic efficiency was limited by the relatively low binding affinity between artificial enzyme and substrate. In this work, substrate l-cysteine (l-Cys) and hemin were combined into one molecule to form l-Cys-hemin/G-quadruplex as an artificial self-catalytic complex for the improvement of the binding affinity between l-Cys-hemin/G-quadruplex and l-Cys. The apparent Michaelis-Menten constant ( K = 2.615 μM) on l-Cys-hemin/G-quadruplex for l-Cys was further investigated to assess the affinity, which was much lower than that of hemin/G-quadruplex ( K = 8.640 μM), confirming l-Cys-hemin/G-quadruplex possessed better affinity to l-Cys compared with that of hemin/G-quadruplex. Meanwhile, l-Cys bilayer could be further assembled onto the surface of l-Cys-hemin/G-quadruplex based on hydrogen-bond and electrostatic interaction to concentrate l-Cys around the active center, which was beneficial to the catalytic enhancement. Through this efficient electrochemical self-catalytic platform, a sensitive thrombin aptasensor was constructed. The results exhibited good sensitivity from 0.1 pM to 80 nM and the detection limit was calculated to be 0.032 pM. This self-catalytic strategy with improved binding affinity between l-Cys-hemin/G-quadruplex and l-Cys could provide an efficient approach to improve artificial enzymatic catalytic efficiency.
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