$Low-flux scanning electron diffraction reveals substructures inside the ordered membrane domain$
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Low-flux scanning electron diffraction reveals substructures inside the ordered membrane domain

Abstract Ordered/disordered phase separation occurring in bio-membranes has piqued researchers’ interest because these ordered domains, called lipid rafts, regulate important biological functions. The structure of the ordered domain has been examined with artificial membranes, which undergo macrosco...

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Autores principales:	Masanao Kinoshita, Shimpei Yamaguchi, Nobuaki Matsumori
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/313cee4a354a4a2e946297a0054a0056
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spelling	oai:doaj.org-article:313cee4a354a4a2e946297a0054a00562021-12-02T11:59:41ZLow-flux scanning electron diffraction reveals substructures inside the ordered membrane domain10.1038/s41598-020-79083-72045-2322https://doaj.org/article/313cee4a354a4a2e946297a0054a00562020-12-01T00:00:00Zhttps://doi.org/10.1038/s41598-020-79083-7https://doaj.org/toc/2045-2322Abstract Ordered/disordered phase separation occurring in bio-membranes has piqued researchers’ interest because these ordered domains, called lipid rafts, regulate important biological functions. The structure of the ordered domain has been examined with artificial membranes, which undergo macroscopic ordered/disordered phase separation. However, owing to technical difficulties, the local structure inside ordered domains remains unknown. In this study, we employed electron diffraction to examine the packing structure of the lipid carbon chains in the ordered domain. First, we prepared dehydrated monolayer samples using a rapid-freezing and sublimation protocol, which attenuates the shrinkage of the chain-packing lattice in the dehydration process. Then, we optimised the electron flux to minimise beam damage to the monolayer sample. Finally, we developed low-flux scanning electron diffraction and assessed the chain packing structure inside the ordered domain formed in a distearoylphosphatidylcholine/dioleoylphosphatidylcholine binary monolayer. Consequently, we discovered that the ordered domain contains multiple subdomains with different crystallographic axes. Moreover, the size of the subdomain is larger in the domain centre than that near the phase boundary. To our knowledge, this is the first study to reveal the chain packing structures inside an ordered domain.Masanao KinoshitaShimpei YamaguchiNobuaki MatsumoriNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 10, Iss 1, Pp 1-11 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Masanao Kinoshita Shimpei Yamaguchi Nobuaki Matsumori Low-flux scanning electron diffraction reveals substructures inside the ordered membrane domain
description	Abstract Ordered/disordered phase separation occurring in bio-membranes has piqued researchers’ interest because these ordered domains, called lipid rafts, regulate important biological functions. The structure of the ordered domain has been examined with artificial membranes, which undergo macroscopic ordered/disordered phase separation. However, owing to technical difficulties, the local structure inside ordered domains remains unknown. In this study, we employed electron diffraction to examine the packing structure of the lipid carbon chains in the ordered domain. First, we prepared dehydrated monolayer samples using a rapid-freezing and sublimation protocol, which attenuates the shrinkage of the chain-packing lattice in the dehydration process. Then, we optimised the electron flux to minimise beam damage to the monolayer sample. Finally, we developed low-flux scanning electron diffraction and assessed the chain packing structure inside the ordered domain formed in a distearoylphosphatidylcholine/dioleoylphosphatidylcholine binary monolayer. Consequently, we discovered that the ordered domain contains multiple subdomains with different crystallographic axes. Moreover, the size of the subdomain is larger in the domain centre than that near the phase boundary. To our knowledge, this is the first study to reveal the chain packing structures inside an ordered domain.
format	article
author	Masanao Kinoshita Shimpei Yamaguchi Nobuaki Matsumori
author_facet	Masanao Kinoshita Shimpei Yamaguchi Nobuaki Matsumori
author_sort	Masanao Kinoshita
title	Low-flux scanning electron diffraction reveals substructures inside the ordered membrane domain
title_short	Low-flux scanning electron diffraction reveals substructures inside the ordered membrane domain
title_full	Low-flux scanning electron diffraction reveals substructures inside the ordered membrane domain
title_fullStr	Low-flux scanning electron diffraction reveals substructures inside the ordered membrane domain
title_full_unstemmed	Low-flux scanning electron diffraction reveals substructures inside the ordered membrane domain
title_sort	low-flux scanning electron diffraction reveals substructures inside the ordered membrane domain
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/313cee4a354a4a2e946297a0054a0056
work_keys_str_mv	AT masanaokinoshita lowfluxscanningelectrondiffractionrevealssubstructuresinsidetheorderedmembranedomain AT shimpeiyamaguchi lowfluxscanningelectrondiffractionrevealssubstructuresinsidetheorderedmembranedomain AT nobuakimatsumori lowfluxscanningelectrondiffractionrevealssubstructuresinsidetheorderedmembranedomain
_version_	1718394739154223104

Low-flux scanning electron diffraction reveals substructures inside the ordered membrane domain

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