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Advances in the Biological Application of Force-Induced Remnant Magnetization Spectroscopy
Biomolecules participate in various physiological and pathological processes through intermolecular interactions generally driven by non-covalent forces. In the present review, the force-induced remnant magnetization spectroscopy (FIRMS) is described and illustrated as a novel method to measure non-...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9000611/ https://www.ncbi.nlm.nih.gov/pubmed/35408471 http://dx.doi.org/10.3390/molecules27072072 |
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author | Liao, Shuyu Sun, Mengxue Zhan, Jinxiu Xu, Min Yao, Li |
author_facet | Liao, Shuyu Sun, Mengxue Zhan, Jinxiu Xu, Min Yao, Li |
author_sort | Liao, Shuyu |
collection | PubMed |
description | Biomolecules participate in various physiological and pathological processes through intermolecular interactions generally driven by non-covalent forces. In the present review, the force-induced remnant magnetization spectroscopy (FIRMS) is described and illustrated as a novel method to measure non-covalent forces. During the FIRMS measurement, the molecular magnetic probes are magnetized to produce an overall magnetization signal. The dissociation under the interference of external force yields a decrease in the magnetic signal, which is recorded and collected by atomic magnetometer in a spectrum to study the biological interactions. Furthermore, the recent FIRMS development with various external mechanical forces and magnetic probes is summarized. |
format | Online Article Text |
id | pubmed-9000611 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-90006112022-04-12 Advances in the Biological Application of Force-Induced Remnant Magnetization Spectroscopy Liao, Shuyu Sun, Mengxue Zhan, Jinxiu Xu, Min Yao, Li Molecules Review Biomolecules participate in various physiological and pathological processes through intermolecular interactions generally driven by non-covalent forces. In the present review, the force-induced remnant magnetization spectroscopy (FIRMS) is described and illustrated as a novel method to measure non-covalent forces. During the FIRMS measurement, the molecular magnetic probes are magnetized to produce an overall magnetization signal. The dissociation under the interference of external force yields a decrease in the magnetic signal, which is recorded and collected by atomic magnetometer in a spectrum to study the biological interactions. Furthermore, the recent FIRMS development with various external mechanical forces and magnetic probes is summarized. MDPI 2022-03-23 /pmc/articles/PMC9000611/ /pubmed/35408471 http://dx.doi.org/10.3390/molecules27072072 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Liao, Shuyu Sun, Mengxue Zhan, Jinxiu Xu, Min Yao, Li Advances in the Biological Application of Force-Induced Remnant Magnetization Spectroscopy |
title | Advances in the Biological Application of Force-Induced Remnant Magnetization Spectroscopy |
title_full | Advances in the Biological Application of Force-Induced Remnant Magnetization Spectroscopy |
title_fullStr | Advances in the Biological Application of Force-Induced Remnant Magnetization Spectroscopy |
title_full_unstemmed | Advances in the Biological Application of Force-Induced Remnant Magnetization Spectroscopy |
title_short | Advances in the Biological Application of Force-Induced Remnant Magnetization Spectroscopy |
title_sort | advances in the biological application of force-induced remnant magnetization spectroscopy |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9000611/ https://www.ncbi.nlm.nih.gov/pubmed/35408471 http://dx.doi.org/10.3390/molecules27072072 |
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