Multi-Level Engineering of Staggered Band Alignment Heterojunctions and Au@CeO2Yolk-Shell Nanozyme for Photoelectrochemical Biosensing Under Zero-Bias Conditions AITranslate
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The integration of artificial nanozymes with photoelectrochemical(PEC)biosensing remains underexplored,primarily due to challenges in balancing catalytic efficiency,material stability,and interfacial charge dynamics.Herein,we present a novel split-type PEC biosensor that leverages Au@CeO2yolk-shell nanozymes with robust phosphatase-mimicking activity and staggered band structure of WO3/BiVO4heterojunction for ultrasensitive detection of the breast cancer biomarker HER-2.Unlike conventional nanoenzymes,the yolk-shell architecture encases AuNPs within a CeO2shell,synergistically enhancing catalytic efficiency by maximizing the active surface area while simultaneously preventing nanoparticle aggregation and leaching through a protective barrier.Density functional theory(DFT)calculations reveal that the CeO2(111)/Au(111)interface drastically reduces the energy barrier for phosphate ester bond cleavage(-16.94 eV vs.5.69 eV for free molecules),thereby enabling rapid hydrolysis of ascorbic acid 2-phosphate(AAP)into ascorbic acid.This catalytic amplification strategy,when integrated with a visible-light-responsive semiconductor substrate,enables zero-bias detection and while effectively eliminating interference from high-voltage operations.The biosensor achieves a detection limit of 41 fg/mL(S/N=3)for HER-2 across a linear range of 0.0001-100 ng/mL,surpassing existing methods.Remarkable selectivity,reproducibility(RSD=3.9%),and recovery rates(95.1%–102.4%)in serum further validate its clinical applicability.This work establishes a universal platform for nanozyme-driven PEC biosensing,presenting significant promise for future use in pathological diagnostics.
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Chinese Library Classification Number:TB383[一般工业技术];TP212.3[一般工业技术—材料科学与工程]
Citation Information:
The integration of artificial nanozymes with photoelectrochemical(PEC)biosensing remains underexplored,primarily due to challenges in balancing catalytic efficiency,material stability,and interfacial charge dynamics.Herein,we present a novel split-type PEC biosensor that leverages Au@CeO2yolk-shell nanozymes with robust phosphatase-mimicking activity and staggered band structure of WO3/BiVO4heterojunction for ultrasensitive detection of the breast cancer biomarker HER-2.Unlike conventional nanoenzymes,the yolk-shell architecture encases AuNPs within a CeO2shell,synergistically enhancing catalytic efficiency by maximizing the active surface area while simultaneously preventing nanoparticle aggregation and leaching through a protective barrier.Density functional theory(DFT)calculations reveal that the CeO2(111)/Au(111)interface drastically reduces the energy barrier for phosphate ester bond cleavage(-16.94 eV vs.5.69 eV for free molecules),thereby enabling rapid hydrolysis of ascorbic acid 2-phosphate(AAP)into ascorbic acid.This catalytic amplification strategy,when integrated with a visible-light-responsive semiconductor substrate,enables zero-bias detection and while effectively eliminating interference from high-voltage operations.The biosensor achieves a detection limit of 41 fg/mL(S/N=3)for HER-2 across a linear range of 0.0001-100 ng/mL,surpassing existing methods.Remarkable selectivity,reproducibility(RSD=3.9%),and recovery rates(95.1%–102.4%)in serum further validate its clinical applicability.This work establishes a universal platform for nanozyme-driven PEC biosensing,presenting significant promise for future use in pathological diagnostics.
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| GB/T 7714-2015 | [1] Yu Du, Rui Feng, Tingting Wu, et al. Journal of Analysis and Testing, 2025(4): 575-583. |
| MLA | [1] Yu Du, et al., Journal of Analysis and Testing, no. 4, 2025, pp. 575-583. |
| APA | [1] Yu Du, Rui Feng, Tingting Wu, Xue Dong, Hongying Jia, Dongquan Leng, Huangxian Ju, & Qin Wei. (2025). Journal of Analysis and Testing(4), 575-583. |
| IEEE | [1] Yu Du, Rui Feng, Tingting Wu, Xue Dong, Hongying Jia, Dongquan Leng, Huangxian Ju, and Qin Wei, Journal of Analysis and Testing, no. 4, pp. 575-583, 2025. |
