Functionalized gold nanoflowers on carbon screen-printed electrodes: an electrochemical platform for biosensing hemagglutinin protein of influenza A H1N1 virus

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The paper develops an electrochemical biosensing platform using functionalized gold nanoflowers deposited on carbon screen-printed electrodes to detect hemagglutinin (H1) from influenza A H1N1, measuring binding-dependent current changes via differential pulse voltammetry. Gold nanoflower conductivity/surface area was enhanced, and functionalization with 4-aminothiophenol decreased charge transfer resistance 100-fold, enabling antibody immobilization against H1 through covalent amide bond formation and blocking with bovine serum albumin to reduce nonspecific binding. Performance was evaluated in artificial saliva across a clinically relevant H1 concentration range, reporting a limit of detection of 19 pg/mL, with an automated microfluidics coupling that preserved signal without a significant drop. The paper does not explicitly discuss endometriosis or adenomyosis; it was included in the corpus via a keyword match in the upstream search index.

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Materials

chemistry Medicinal and pharmaceutical chemistry Nano- and molecular-scale electronics Nano-biomaterials and bioscience Nanomagnetics Nanomaterials, thin films and nanointerfaces Nanomedicine Nanometrology and nanomechanics Nano-optics Nanopatterning, self-assembly and nanofabrication Nanostructures for energy and sensing applications Natural products chemistry Organo main group chemistry Other nanotechnology (unclassified) Other organic chemistry (unclassified) Photochemistry and photovoltaics Physical organic chemistry Supramolecular chemistry An electrochemical biosensor based on modified carbon screen-printed electrodes (CSPE) was developed for the detection of hemagglutinin of influenza A H1N1 virus (H1). Gold nanoflowers were electrodeposited on the electrode to increase conductivity and surface area. The electrochemical signal was amplified by functionalization of the gold nanoflowers with 4-aminothiophenol, which resulted in a 100-fold decrease of the charge transfer resistance due to a tunneling effect. Subsequently, monoclonal antibodies against H1 were immobilized on the surface via covalent amide bond formation, followed by blocking with bovine serum albumin to minimize nonspecific hydrophobic binding. The electrodes were characterized by cyclic voltammetry and electrochemical impedance spectroscopy experiments in presence of [Fe(CN)6]3−/4−. Differential pulse voltammetry was used to measure the change in current across the electrode as a function of H1 concentration. This was performed on a series of samples of artificial saliva containing H1 protein in a clinically relevant concentration range. In these experiments, the biosensor showed a limit of detection of 19 pg/mL. Finally, the biosensor platform was coupled to an automated microfluidics system and no significant decrease of the electrochemical signal was observed.

Keywords

Electrodeposition; cyclic voltammetry; electrochemical impedance spectroscopy; differential pulse voltammetry; charge transfer. | Format: DOCX | Size: 305.9 KB | Download | When a peer-reviewed version of this preprint is available, this information will be updated in the information box above. If no peer-reviewed version is available, please cite this preprint using the following information: Torres Méndez, C. E.; Nandi, S.; Martinovic, K.; Kühne, P.; Liu, Y.; Taylor, S.; Lysandrou, M.; Romeyro Mascarenhas, M. I. B.; Langwallner, V.; Sebastián Alonso, J. E.; Jovanovic, I.; Lüftner, M.; Gkountana, G.-V.; Bern, D.; Atif, A.-R.; Manouchehri Doulabi, E.; Mestres, G.; Kamali-Moghaddam, M. Beilstein Arch. 2025, 20251. doi:10.3762/bxiv.2025.1.v1 Citation data can be downloaded as file using the "Download" button or used for copy/paste from the text window below. Citation data in RIS format can be imported by all major citation management software, including EndNote, ProCite, RefWorks, and Zotero. © 2025 Torres Méndez et al.; licensee Beilstein-Institut. This is an open access work licensed under the terms of the Beilstein-Institut Open Access License Agreement (https://www.beilstein-archives.org/xiv/terms), which is identical to the Creative Commons Attribution 4.0 International License (https://creativecommons.org/licenses/by/4.0). The reuse of material under this license requires that the author(s), source and license are credited. Third-party material in this work could be subject to other licenses (typically indicated in the credit line), and in this case, users are required to obtain permission from the license holder to reuse the material.

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