Infrared nanospectroscopy study of the light-induced conformational changes of Channelrhodopsin

The channelrhodopsin-ChR2 is a light-sensitive transmembrane protein that acts as a selective ion channel between the intra- and the extra-cellular environments. In the last decade, ChR2 has proven to be essential for optogenetics, because, if expressed in mammalian neural cells, it enables the cont...

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Autores principales:	Temperini Maria Eleonora, Polito Raffaella, Intze Antonia, Schade Ulrich, Puskar Ljljana, Ritter Eglof, Baldassarre Leonetta, Ortolani Michele, Giliberti Valeria
Formato:	article
Lenguaje:	EN
Publicado:	EDP Sciences 2021
Materias:	Physics QC1-999
Acceso en línea:	https://doaj.org/article/76c8ea761674477d9204a57db9534a67
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spelling	oai:doaj.org-article:76c8ea761674477d9204a57db9534a672021-12-02T17:12:51ZInfrared nanospectroscopy study of the light-induced conformational changes of Channelrhodopsin2100-014X10.1051/epjconf/202125513001https://doaj.org/article/76c8ea761674477d9204a57db9534a672021-01-01T00:00:00Zhttps://www.epj-conferences.org/articles/epjconf/pdf/2021/09/epjconf_eosam2021_13001.pdfhttps://doaj.org/toc/2100-014XThe channelrhodopsin-ChR2 is a light-sensitive transmembrane protein that acts as a selective ion channel between the intra- and the extra-cellular environments. In the last decade, ChR2 has proven to be essential for optogenetics, because, if expressed in mammalian neural cells, it enables the control of neuronal activity in response to visible light. Mid-infrared difference spectroscopy can probe the functional conformational changes of light-sensitive proteins, however intrinsic limitations of standard IR spectroscopy in terms of diffraction, and therefore number of probed proteins, require that the mid-IR experiments be performed on huge numbers of lipid membrane patches with overexpressed proteins. In this work, we apply for the first time IR difference nanospectroscopy, based on the use of mid-IR lasers and an atomic force microscope (AFM), to single membrane patches containing ChR2, obtaining relevant spectroscopy results for optogenetic applications and, more generally, for future experimental studies of light-sensitive proteins at the nanoscale.Temperini Maria EleonoraPolito RaffaellaIntze AntoniaSchade UlrichPuskar LjljanaRitter EglofBaldassarre LeonettaOrtolani MicheleGiliberti ValeriaEDP SciencesarticlePhysicsQC1-999ENEPJ Web of Conferences, Vol 255, p 13001 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Physics QC1-999
spellingShingle	Physics QC1-999 Temperini Maria Eleonora Polito Raffaella Intze Antonia Schade Ulrich Puskar Ljljana Ritter Eglof Baldassarre Leonetta Ortolani Michele Giliberti Valeria Infrared nanospectroscopy study of the light-induced conformational changes of Channelrhodopsin
description	The channelrhodopsin-ChR2 is a light-sensitive transmembrane protein that acts as a selective ion channel between the intra- and the extra-cellular environments. In the last decade, ChR2 has proven to be essential for optogenetics, because, if expressed in mammalian neural cells, it enables the control of neuronal activity in response to visible light. Mid-infrared difference spectroscopy can probe the functional conformational changes of light-sensitive proteins, however intrinsic limitations of standard IR spectroscopy in terms of diffraction, and therefore number of probed proteins, require that the mid-IR experiments be performed on huge numbers of lipid membrane patches with overexpressed proteins. In this work, we apply for the first time IR difference nanospectroscopy, based on the use of mid-IR lasers and an atomic force microscope (AFM), to single membrane patches containing ChR2, obtaining relevant spectroscopy results for optogenetic applications and, more generally, for future experimental studies of light-sensitive proteins at the nanoscale.
format	article
author	Temperini Maria Eleonora Polito Raffaella Intze Antonia Schade Ulrich Puskar Ljljana Ritter Eglof Baldassarre Leonetta Ortolani Michele Giliberti Valeria
author_facet	Temperini Maria Eleonora Polito Raffaella Intze Antonia Schade Ulrich Puskar Ljljana Ritter Eglof Baldassarre Leonetta Ortolani Michele Giliberti Valeria
author_sort	Temperini Maria Eleonora
title	Infrared nanospectroscopy study of the light-induced conformational changes of Channelrhodopsin
title_short	Infrared nanospectroscopy study of the light-induced conformational changes of Channelrhodopsin
title_full	Infrared nanospectroscopy study of the light-induced conformational changes of Channelrhodopsin
title_fullStr	Infrared nanospectroscopy study of the light-induced conformational changes of Channelrhodopsin
title_full_unstemmed	Infrared nanospectroscopy study of the light-induced conformational changes of Channelrhodopsin
title_sort	infrared nanospectroscopy study of the light-induced conformational changes of channelrhodopsin
publisher	EDP Sciences
publishDate	2021
url	https://doaj.org/article/76c8ea761674477d9204a57db9534a67
work_keys_str_mv	AT temperinimariaeleonora infrarednanospectroscopystudyofthelightinducedconformationalchangesofchannelrhodopsin AT politoraffaella infrarednanospectroscopystudyofthelightinducedconformationalchangesofchannelrhodopsin AT intzeantonia infrarednanospectroscopystudyofthelightinducedconformationalchangesofchannelrhodopsin AT schadeulrich infrarednanospectroscopystudyofthelightinducedconformationalchangesofchannelrhodopsin AT puskarljljana infrarednanospectroscopystudyofthelightinducedconformationalchangesofchannelrhodopsin AT rittereglof infrarednanospectroscopystudyofthelightinducedconformationalchangesofchannelrhodopsin AT baldassarreleonetta infrarednanospectroscopystudyofthelightinducedconformationalchangesofchannelrhodopsin AT ortolanimichele infrarednanospectroscopystudyofthelightinducedconformationalchangesofchannelrhodopsin AT gilibertivaleria infrarednanospectroscopystudyofthelightinducedconformationalchangesofchannelrhodopsin
_version_	1718381385748578304

Infrared nanospectroscopy study of the light-induced conformational changes of Channelrhodopsin

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