Peptide-antifouling interface for monitoring fi-amyloid based on electrochemiluminescence resonance energy transfer
关键字：BETA; IDENTIFICATION; IMMUNOSENSOR; LUMINOL; DESIGN
摘要：In this study, a novel antifouling electrochemiluminescence (ECL) analytical platform has been developed for the highly sensitive quantification of fi-amyloid (Afi) peptides based on the ECL resonance energy transfer (ECL-RET) mechanism. Specifically, glassy carbon electrodes (GCE) were initially coated with graphite -phase carbon nitride (g-C3N4) nanosheets, followed by the electropolymerization of polyaniline (PANI) onto the electrode surface. Subsequently, a promising peptide motif candidate (COOH-CPPPPDKDKDKDKKLVFF) was immobilized onto the PANI-modified electrode, functioning as a critical component for both antifouling and specific recognition of fulllength Afi peptides. Furthermore, this peptide motif demonstrated inhibitory effects on Afi aggregation and dissociation. Upon immobilization of the peptide motif, Afi aptamer-CdS QDs were bound to the electrode surface through peptide-specific interactions with A beta, thereby facilitating the highly sensitive ECL detection of Afi. Under the optimal conditions, the proposed biosensor exhibited an Afi detection range from 0.1 pM to 100 nM with a detection limit of 16.1 fM. As such, this innovative platform offers a straightforward approach to antifouling, quantification, and monitoring of Afi concentrations in the blood samples.
卷号：267
期号：
是否译文：否
