Peptide-antifouling interface for monitoring β-amyloid based on electrochemiluminescence resonance energy transfer

Abstract

In this study, a novel antifouling electrochemiluminescence (ECL) analytical platform has been developed for the highly sensitive quantification of β-amyloid (Aβ) 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 full-length Aβ peptides. Furthermore, this peptide motif demonstrated inhibitory effects on Aβ aggregation and dissociation. Upon immobilization of the peptide motif, Aβ aptamer-CdS QDs were bound to the electrode surface through peptide-specific interactions with Aβ, thereby facilitating the highly sensitive ECL detection of Aβ. Under the optimal conditions, the proposed biosensor exhibited an Aβ 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 Aβ concentrations in the blood samples.