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Proteinoid Microspheres as Protoneural Networks

[Image: see text] Proteinoids, also known as thermal proteins, possess a fascinating ability to generate microspheres that exhibit electrical spikes resembling the action potentials of neurons. These spiking microspheres, referred to as protoneurons, hold the potential to assemble into proto-nanobra...

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Detalles Bibliográficos
Autores principales: Mougkogiannis, Panagiotis, Adamatzky, Andrew
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2023
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10536103/
https://www.ncbi.nlm.nih.gov/pubmed/37780014
http://dx.doi.org/10.1021/acsomega.3c05670
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author Mougkogiannis, Panagiotis
Adamatzky, Andrew
author_facet Mougkogiannis, Panagiotis
Adamatzky, Andrew
author_sort Mougkogiannis, Panagiotis
collection PubMed
description [Image: see text] Proteinoids, also known as thermal proteins, possess a fascinating ability to generate microspheres that exhibit electrical spikes resembling the action potentials of neurons. These spiking microspheres, referred to as protoneurons, hold the potential to assemble into proto-nanobrains. In our study, we investigate the feasibility of utilizing a promising electrochemical technique called differential pulse voltammetry (DPV) to interface with proteinoid nanobrains. We evaluate DPV’s suitability by examining critical parameters such as selectivity, sensitivity, and linearity of the electrochemical responses. The research systematically explores the influence of various operational factors, including pulse width, pulse amplitude, scan rate, and scan time. Encouragingly, our findings indicate that DPV exhibits significant potential as an efficient electrochemical interface for proteinoid nanobrains. This technology opens up new avenues for developing artificial neural networks with broad applications across diverse fields of research.
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spelling pubmed-105361032023-09-29 Proteinoid Microspheres as Protoneural Networks Mougkogiannis, Panagiotis Adamatzky, Andrew ACS Omega [Image: see text] Proteinoids, also known as thermal proteins, possess a fascinating ability to generate microspheres that exhibit electrical spikes resembling the action potentials of neurons. These spiking microspheres, referred to as protoneurons, hold the potential to assemble into proto-nanobrains. In our study, we investigate the feasibility of utilizing a promising electrochemical technique called differential pulse voltammetry (DPV) to interface with proteinoid nanobrains. We evaluate DPV’s suitability by examining critical parameters such as selectivity, sensitivity, and linearity of the electrochemical responses. The research systematically explores the influence of various operational factors, including pulse width, pulse amplitude, scan rate, and scan time. Encouragingly, our findings indicate that DPV exhibits significant potential as an efficient electrochemical interface for proteinoid nanobrains. This technology opens up new avenues for developing artificial neural networks with broad applications across diverse fields of research. American Chemical Society 2023-09-12 /pmc/articles/PMC10536103/ /pubmed/37780014 http://dx.doi.org/10.1021/acsomega.3c05670 Text en © 2023 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by/4.0/Permits the broadest form of re-use including for commercial purposes, provided that author attribution and integrity are maintained (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Mougkogiannis, Panagiotis
Adamatzky, Andrew
Proteinoid Microspheres as Protoneural Networks
title Proteinoid Microspheres as Protoneural Networks
title_full Proteinoid Microspheres as Protoneural Networks
title_fullStr Proteinoid Microspheres as Protoneural Networks
title_full_unstemmed Proteinoid Microspheres as Protoneural Networks
title_short Proteinoid Microspheres as Protoneural Networks
title_sort proteinoid microspheres as protoneural networks
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10536103/
https://www.ncbi.nlm.nih.gov/pubmed/37780014
http://dx.doi.org/10.1021/acsomega.3c05670
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