Advancements in the provision of deuterated lipids for neutron applications from the National Deuteration Facility

Simple item page
dc.contributor.authorYepuri, NRen_AU
dc.contributor.authorMoir, Men_AU
dc.contributor.authorKrause-Heuer, AMen_AU
dc.contributor.authorKlenner, MAen_AU
dc.contributor.authorDarwish, TAen_AU
dc.date.accessioned2023-05-05T00:54:10Zen_AU
dc.date.available2023-05-05T00:54:10Zen_AU
dc.date.issued2020-11-11en_AU
dc.date.statistics2023-04-19en_AU
dc.description.abstractMolecular deuteration significantly increases the options for structure-function investigations using neutron scattering and diffraction techniques. Chemical deuteration activities, where catalysed 1H/2H exchange is followed by custom chemical synthesis, have led to diverse neutron scattering and reflectometry studies previously hampered by the lack of appropriate scattering contrast in multi-component samples. Deuteration of phospholipids is a common practice to elucidate membrane structure, dynamics and function, by providing selective visualisation in neutron scattering. Although analogous deuterium? (2H) and hydrogen? containing (1H) molecules have similar physicochemical properties, these isotopes of hydrogen result in vastly different for neutron scattering signals. Over the past few years the National Deuteration Facility (ANSTO) has increased its synthetic capability to produce complex deuterated molecules including lipids and phospholipids. Such synthetically challenging molecules are perdeuterated phytantriol1, tail deuterated POPC, and perdeuterated POPC.2 Phytantriol is an interfacially-active lipid that is chemically robust, non-digestible and forms particles with internal bicontinuous cubic phase structures (cubosomes) when dispersed with non-ionic surfactants at physiological temperatures. The tail-deuterated POPC, perdeuterated POPC and tail-deuterated GMO isotopologues would also provide suitable contrast for many neutron experiments and so these have been also our synthetic targets. Recently neutron reflection was employed to investigate the impact of phospholipid saturation (POPC-d64) and presence of cholesterol in cell model membranes on LDL and HDL lipid exchange and removal processes.3 Neutron reflection data that distinguish the effect of phospholipid acyl chain saturation and the presence of cholesterol on the ability of lipoproteins to exchange lipids to/from model membrane will be presented.en_AU
dc.identifier.citationYepuri, R., Moir, M., Krause-Heuer, A., Klenner, M., & Darwish, T. (2020). Advancements in the provision of deuterated lipids for neutron applications from the National Deuteration Facility. Paper presented to the ANBUG-AINSE Neutron Scattering Symposium, AANSS 2020, Virtual Meeting, 11th - 13th November 2020, (pp. 18). Retrieved from: https://events01.synchrotron.org.au/event/125/attachments/725/1149/AANSS_Abstract_Booklet_Complete_-_1_Page_Reduced.pdfen_AU
dc.identifier.conferenceenddate13 November 2020en_AU
dc.identifier.conferencenameANBUG-AINSE Neutron Scattering Symposium, AANSS 2020en_AU
dc.identifier.conferenceplaceVirtual Meetingen_AU
dc.identifier.conferencestartdate11 November 2020en_AU
dc.identifier.pagination18en_AU
dc.identifier.urihttps://events01.synchrotron.org.au/event/125/attachments/725/1149/AANSS_Abstract_Booklet_Complete_-_1_Page_Reduced.pdfen_AU
dc.identifier.urihttps://apo.ansto.gov.au/dspace/handle/10238/15002en_AU
dc.language.isoenen_AU
dc.publisherAustralian Institute of Nuclear Science and Engineering (AINSE)en_AU
dc.subjectScatteringen_AU
dc.subjectCatalysisen_AU
dc.subjectIsotopesen_AU
dc.subjectHydrogenen_AU
dc.subjectPhospholipidsen_AU
dc.subjectStructure functionsen_AU
dc.titleAdvancements in the provision of deuterated lipids for neutron applications from the National Deuteration Facilityen_AU
dc.typeConference Abstracten_AU
Files
Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
contribution (1).pdf
Size:
38.04 KB
Format:
Adobe Portable Document Format
Description:
Download
License bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
license.txt
Size:
1.63 KB
Format:
Item-specific license agreed upon to submission
Description:
Download
Collections
Conference Publications