Determining the location of encapsulated peptides, proteins, and other biomolecules in contrast-matched lipid bicontinuous cubic phases using SANS

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dc.contributor.authorvan't Hag, Len_AU
dc.contributor.authorde Campo, Len_AU
dc.contributor.authorGras, Sen_AU
dc.contributor.authorDrummond, CJen_AU
dc.contributor.authorConn, Cen_AU
dc.date.accessioned2021-08-09T22:30:27Zen_AU
dc.date.available2021-08-09T22:30:27Zen_AU
dc.date.issued2017-07-12en_AU
dc.date.statistics2021-08-09en_AU
dc.description.abstractTo evolve biological and biomedical applications of hybrid biomolecule?lipid materials, including in meso protein crystallization and drug delivery, an understanding of the location of the biomolecules within the bicontinuous cubic phases is crucial. Theoretical modeling has indicated that proteins and additive lipids might phase separate locally and adopt a preferred location in the cubic phase, but this has never been experimentally confirmed. We have shown that perfectly contrast-matched cubic phases in D2O can be studied using SANS by mixing fully deuterated and hydrogenated lipid. The model transmembrane peptide WALP21 showed no preferential location in the membrane of the diamond and gyroid cubic phases of phytanoyl monoethanolamide [L. van ‘t Hag et al, J. Phys. Chem. Lett. 2016, 7(14), 2862-2866]. In addition, this result opens up the possibility of studying the conformation (and hence function) of amphiphilic proteins and peptides within a lipid bilayer environment. The effect of deuteration on the cubic phase forming lipid was also investigated to advance the use of neutron scattering techniques to study soft matter systems. Additionally, we have performed extensive characterizations of the cubic phase nanostructure subsequent to protein and peptide incorporation using synchrotron SAXS, as well as the protein and peptide secondary structures using synchrotron circular dichroism spectroscopy [L. van ‘t Hag et al, Langmuir, 2016, 32(27), 6882-6894].en_AU
dc.identifier.citationvan't Hag, L., de Campo, L., Gras, S., Drummond, C., & Conn, C. (2017). Determining the location of encapsulated peptides, proteins, and other biomolecules in contrast-matched lipid bicontinuous cubic phases using SANS. Paper presented at ICNS 2017 (International Conference on Neutron Scattering), Daejeon, South Korea, 9 to 13 July 2017. Retrieved from: http://www.icns2017.org/program.phpen_AU
dc.identifier.conferenceenddate13 July 2017en_AU
dc.identifier.conferencenameICNS 2017 (International Conference on Neutron Scattering)en_AU
dc.identifier.conferenceplaceDaejeon, South Koreaen_AU
dc.identifier.conferencestartdate9 July 2017en_AU
dc.identifier.urihttp://www.icns2017.org/program.phpen_AU
dc.identifier.urihttps://apo.ansto.gov.au/dspace/handle/10238/11285en_AU
dc.language.isoenen_AU
dc.publisherInternational Conference on Neutron Scatteringen_AU
dc.subjectLipidsen_AU
dc.subjectDrug deliveryen_AU
dc.subjectSpectroscopyen_AU
dc.subjectDichroismen_AU
dc.subjectNeutron diffractionen_AU
dc.subjectCrystallizationen_AU
dc.subjectPeptidesen_AU
dc.titleDetermining the location of encapsulated peptides, proteins, and other biomolecules in contrast-matched lipid bicontinuous cubic phases using SANSen_AU
dc.typeConference Abstracten_AU
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