Currently available methods for detecting amyloid β (Aβ) derivatives are mainly dedicated to determining the long forms Aβ1-42 and Aβ1-40. At the same time, the number of physiologically occurring Aβ analogs is much higher, including those truncated at the N- and C-termini. Their identification using standard methods is challenging due to the structural similarity of various Aβ analogs, but could highly benefit from both biomarkers discovery and pathophysiological studies of Alzheimer's disease. Therefore a "chemical tongue" sensing strategy was employed for the detection of seven Aβ peptide derivatives: Aβ1-16, Aβ4-16, Aβ4-9, Aβ5-16, Aβ5-12, Aβ5-9, Aβ12-16. The proposed sensing system is based on competitive interactions between quantum dots, Cu(II) ions, and Aβ peptides, providing unique fluorescence fingerprints useful for the identification of analytes. After carefully evaluating the Aβ sample preparation protocol, perfect determination of all studied Aβ peptides was achieved using partial least square-discriminant analysis (PLS-DA). The developed PLS-DA models are characterized by excellent accuracy, sensitivity, precision, and specificity of analyte determination, emphasizing the potential of the proposed sensing strategy.
Keywords: Amyloid β; Chemical tongue; Competitive assay; Multispectral fluorescence; PLS-DA; Quantum dots.
© 2024. The Author(s).