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Published on: December 2, 2022
A dual-mode electrochemiluminescence/SERS biosensor for B-type natriuretic peptide based on a T7-CRISPR/Cas13a
Yang Li1, Haozhen Ren1, Runze Wu2
1Guangxi Key Laboratory for Preclinical and Translational Research on Bone and Joint Degenerative Diseases, Affiliated Hospital of Youjiang Medical University for Nationalities, BaiSe, Guangxi, 533000, China; Key Laboratory of Guangxi's Colleges for the Study of Characteristic Ethnic Medicine in Youjiang River Basin, Youjiang Medical University for Nationalities, Baise, Guangxi, 533000, China.
Abstract:
B-type natriuretic peptide (BNP) is an important biomarker for cardiovascular diseases, motivating sensitive and robust quantification in complex matrices. Here we report a single-electrode, anti-correlated dual-mode electrochemiluminescence/surface-enhanced Raman scattering (ECL/SERS) biosensor that couples split-aptamer recognition with a solution-phase T7 transcription-CRISPR/Cas13a cascade and an interfacial toehold-mediated strand-displacement "probe-stripping" transduction on a CsPbBr3@PDA@Au-modified glassy carbon electrode. BNP binding releases an active T7 template to generate trigger RNA, which activates Cas13a collateral cleavage to produce initiator strands for interfacial unlocking. The interface reaction removes ferrocene/Raman co-labeled probes, synchronizing ECL turn-on with SERS turn-off and enabling ratiometric quantification (R = IECL/ISERS) to suppress common-mode variability. The sensor provides BNP determination over 0-106 aM with log-linear single-mode calibrations and a continuous ratiometric response. Selectivity was validated against multiple interferents and the structurally related peptide NT-proBNP at the same concentration (106 aM), showing negligible ratiometric change relative to BNP. Serum-sample evaluation and stability tests further support feasibility in complex matrices. This work establishes a cascade-to-interface ratiometric strategy for robust protein biosensing.
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