Triglyceride-Tethered Membrane Lipase Sensor.

Lankage, UM; Holt, SA; Bridge, S; Cornell, B; Cranfield, CG

Triglyceride-Tethered Membrane Lipase Sensor.

Lankage, UM Holt, SA Bridge, S Cornell, B Cranfield, CG

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Publisher:: American Chemical Society (ACS)
Publication Type:: Journal Article
Citation:: ACS Appl Mater Interfaces, 2023
Issue Date:: 2023-11-06

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Field	Value	Language
dc.contributor.author	Lankage, UM
dc.contributor.author	Holt, SA
dc.contributor.author	Bridge, S
dc.contributor.author	Cornell, B
dc.contributor.author	Cranfield, CG
dc.date.accessioned	2023-11-14T21:42:32Z
dc.date.available	2023-11-14T21:42:32Z
dc.date.issued	2023-11-06
dc.identifier.citation	ACS Appl Mater Interfaces, 2023
dc.identifier.issn	1944-8244
dc.identifier.issn	1944-8252
dc.identifier.uri	http://hdl.handle.net/10453/173413
dc.description.abstract	Sensors that can quickly measure the lipase activity from biological samples are useful in enzyme production and medical diagnostics. However, current lipase sensors have limitations such as requiring fluorescent labels, pH control of buffer vehicles, or lengthy assay preparation. We introduce a sparsely tethered triglyceride substrate anchored off of a gold electrode for the impedance sensing of real-time lipase activity. The tethered substrate is self-assembled using a rapid solvent exchange technique and can form an anchored bilayer 1 nm off the gold electrode. This allows for an aqueous reservoir region, providing access to ions transported through membrane defects caused by triglyceride enzymatic hydrolysis. Electrical impedance spectroscopy techniques can readily detect the decrease in resistance caused by enzymatically induced defects. This rapid and reliable lipase detection method can have potential applications in disease studies, monitoring of lipase production, and as point-of-care diagnostic devices.
dc.format	Print-Electronic
dc.language	eng
dc.publisher	American Chemical Society (ACS)
dc.relation	http://purl.org/au-research/grants/arc/IH150100028
dc.relation.ispartof	ACS Appl Mater Interfaces
dc.relation.isbasedon	10.1021/acsami.3c11767
dc.rights	info:eu-repo/semantics/openAccess
dc.subject	03 Chemical Sciences, 09 Engineering
dc.subject.classification	Nanoscience & Nanotechnology
dc.subject.classification	34 Chemical sciences
dc.subject.classification	40 Engineering
dc.subject.classification	51 Physical sciences
dc.title	Triglyceride-Tethered Membrane Lipase Sensor.
dc.type	Journal Article
utslib.location.activity	United States
utslib.for	03 Chemical Sciences
utslib.for	09 Engineering
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Strength - CHT - Health Technologies
pubs.organisational-group	/University of Technology Sydney/Faculty of Science/School of Life Sciences
pubs.organisational-group	/University of Technology Sydney/Centre for Health Technologies (CHT)
utslib.copyright.status	open_access	*
dc.date.updated	2023-11-14T21:42:30Z
pubs.publication-status	Published online

Abstract:

Sensors that can quickly measure the lipase activity from biological samples are useful in enzyme production and medical diagnostics. However, current lipase sensors have limitations such as requiring fluorescent labels, pH control of buffer vehicles, or lengthy assay preparation. We introduce a sparsely tethered triglyceride substrate anchored off of a gold electrode for the impedance sensing of real-time lipase activity. The tethered substrate is self-assembled using a rapid solvent exchange technique and can form an anchored bilayer 1 nm off the gold electrode. This allows for an aqueous reservoir region, providing access to ions transported through membrane defects caused by triglyceride enzymatic hydrolysis. Electrical impedance spectroscopy techniques can readily detect the decrease in resistance caused by enzymatically induced defects. This rapid and reliable lipase detection method can have potential applications in disease studies, monitoring of lipase production, and as point-of-care diagnostic devices.

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http://hdl.handle.net/10453/173413