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1.
ACS Sens ; 9(3): 1475-1481, 2024 Mar 22.
Artículo en Inglés | MEDLINE | ID: mdl-38441485

RESUMEN

As a tumor-suppressing protein, p53 plays a crucial role in preventing cancer development. Its utility as an early cancer detection tool is significant, potentially enabling clinicians to forestall disease advancement and improve patient prognosis. In response to the pathological overexpression of this antigen in tumors, the prevalence of anti-p53 antibodies increases in serum, in a manner quantitatively indicative of cancer progression. This spike can be detected through techniques, such as Western blotting, immunohistochemistry, and immunoprecipitation. In this study, we present an electrochemical approach that supports ultrasensitive and highly selective anti-p53 autoantibody quantification without the use of an immuno-modified electrode. We specifically employ antigen-mimicking and antibody-capturing peptide-coated magnetic nanoparticles, along with an AC magnetic field-promoted sample mixing, prior to the presentation of Fab-captured targets to simple lectin-modified sensors. The subfemtomolar assays are highly selective and support quantification from serum-spiked samples within minutes.


Asunto(s)
Antígenos de Neoplasias , Autoanticuerpos , Nanopartículas de Magnetita , Imitación Molecular , Neoplasias , Proteína p53 Supresora de Tumor , Humanos , Neoplasias/diagnóstico , Proteína p53 Supresora de Tumor/inmunología , Autoanticuerpos/sangre , Antígenos de Neoplasias/inmunología , Técnicas Biosensibles , Detección Precoz del Cáncer
2.
Anal Chem ; 95(10): 4721-4727, 2023 03 14.
Artículo en Inglés | MEDLINE | ID: mdl-36856747

RESUMEN

We introduce a facile assessment of binding kinetics at bioreceptive redox-active interfaces as a means of quantifying target proteins. This is achieved by monitoring the redox capacitance (Cr) of a receptor-modified conductive polymer interface under continuous flow. Exemplified with the quantification of C-reactive protein (CRP), capacitance analyses resolve both the association and dissociation regimes in real-time. Significantly, the rate of electrochemical signal change within the association regime is a sensitive function of target concentration, enabling marker assaying down to picomolar levels, comparable to end-point assays, in 15 s. This reagentless proof-of-principle methodology is envisioned to be widely applicable to the facile quantification of a range of other pertinent, clinically relevant targets.


Asunto(s)
Técnicas Biosensibles , Cinética , Técnicas Biosensibles/métodos , Biomarcadores/análisis , Proteína C-Reactiva/análisis , Oxidación-Reducción
3.
J Phys Chem Lett ; 13(1): 291-295, 2022 Jan 13.
Artículo en Inglés | MEDLINE | ID: mdl-34978829

RESUMEN

The superatomic orbital splitting (SOS) method is developed to understand the electronic structures of coinage metal nanoclusters, in which delocalized electron counts are not magic numbers. Because the symmetry of a metal core can significantly affect the electronic structure of a nanocluster, this method takes the shape of the core into account in determining the order of group orbital levels. By taking nanoclusters as superatoms, a highly positively charged core is established by removing the ligands and staples. The superatomic orbitals split into group orbitals at different energy levels because of the nonspherical shape of the cluster core. Therefore, the electron configuration of the nonmagic-number nanocluster can be qualitatively analyzed without quantum chemical calculations, which is very important for understanding the stability of the cluster.

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