NDLI: Direct demonstration of lipid phosphorylation in the lipid bilayer of the biomimetic bicontinuous cubic phase using the confined enzyme lipid A phosphoethanolamine transferase

Please wait, while we are loading the content...

Two- and three-phase equilibria of polydisperse Yukawa hard-sphere fluids confined in random porous media: high temperature approximation and scaled particle theory

Active gas replenishment and sensing of the wetting state in a submerged superhydrophobic surface

From geometric optics to plants: the eikonal equation for buckling

Integration of colloids into a semi-flexible network of fibrin

Direct visualization of particle attachment to a pendant drop

Clathrin polymerization exhibits high mechano-geometric sensitivity

Phase diagram of elastic spheres

A dissipative particle dynamics study of a flexible filament in confined shear flow

Interfacial rheology of coexisting solid and fluid monolayers

Direct demonstration of lipid phosphorylation in the lipid bilayer of the biomimetic bicontinuous cubic phase using the confined enzyme lipid A phosphoethanolamine transferase

Microfluidic pumping by micromolar salt concentrations

Back cover

Soft Matter Vol - 13 Issue - 6

Soft Matter Vol - 13 Issue - 5

Soft Matter Vol - 13 Issue - 4

Soft Matter Vol - 13 Issue - 3

Soft Matter Vol - 13 Issue - 2

Direct demonstration of lipid phosphorylation in the lipid bilayer of the biomimetic bicontinuous cubic phase using the confined enzyme lipid A phosphoethanolamine transferase

Content Provider	Royal Society of Chemistry (RSC)
Author	Hag, Leonie ’t Seabrook, Shane A. Drummond, Calum J. Vrielink, Alice Conn, Charlotte E. Anandan, Anandhi Gras, Sally L.
Copyright Year	2017
Abstract	Retention of amphiphilic protein activity within the lipid bilayer membrane of the nanostructured biomimetic bicontinuous cubic phase is crucial for applications utilizing these hybrid protein–lipid self-assembly materials, such as in meso membrane protein crystallization and drug delivery. Previous work, mainly on soluble and membrane-associated enzymes, has shown that enzyme activity may be modified when immobilized, including membrane bound enzymes. The effect on activity may be even greater for amphiphilic enzymes with a large hydrophilic domain, such as the Neisserial enzyme lipid A phosphoethanolamine transferase (EptA). Encapsulation within the biomimetic but non-endogenous lipid bilayer membrane environment may modify the enzyme conformation, while confinement of the large hydrophilic domain with the nanoscale water channels of a continuous lipid bilayer structure may prevent full function of this enzyme. Herein we show that NmEptA remains active despite encapsulation within a nanostructured bicontinuous cubic phase. Full transfer of the phosphoethanolamine (PEA) group from a 1,2-dioleoyl-glycero-phosphoethanolamine (DOPE) doped lipid to monoolein (MO), which makes up the bicontinuous cubic phase, is shown. The reaction was found to be non-specific to the alkyl chain identity. The observed rate of enzyme activity is similar to other membrane bound enzymes, with complete transfer of the PEA group occurring in vitro, under the conditions studied, over a 24 hour timescale.
Starting Page	1493
Ending Page	1504
Page Count	12
File Format	HTM / HTML PDF
ISSN	1744683X
Volume Number	13
Issue Number	7
Journal	Soft Matter
DOI	10.1039/c6sm02487d
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Membrane protein Protein crystallization Enzyme Transferase Drug delivery PEA Lipid A Lipid Self-assembly Biomimetics Alkyl Lipid bilayer EptA Amphiphile Hydrophile Protein structure
Content Type	Text
Resource Type	Article
Subject	Chemistry Condensed Matter Physics

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Cell membrane-inspired polymeric micelles as carriers for drug delivery

Incorporation of the dopamine D2L receptor and bacteriorhodopsin within bicontinuous cubic lipid phases. 1. Relevance to in meso crystallization of integral membrane proteins in monoolein systems

Power struggles in peptide-amphiphile nanostructures

Membrane Protein Structures in Lipid Bilayers; Small-Angle Neutron Scattering With Contrast-Matched Bicontinuous Cubic Phases

Self-assembly and applications of biomimetic and bioactive peptide-amphiphiles

Biomimetic Hierarchical Superstructures: Approaches Using Bicontinuous Microemulsions and Electrodeposition

Self-assembly of amphiphilic peptides

Structure-Function Relationships of the Neisserial EptA Enzyme Responsible for Phosphoethanolamine Decoration of Lipid A: Rationale for Drug Targeting

Regulatory Landscape of the Pseudomonas aeruginosa Phosphoethanolamine Transferase Gene eptA in the Context of Colistin Resistance.

Direct demonstration of lipid phosphorylation in the lipid bilayer of the biomimetic bicontinuous cubic phase using the confined enzyme lipid A phosphoethanolamine transferase

Similar Documents

Cell membrane-inspired polymeric micelles as carriers for drug delivery

Incorporation of the dopamine D2L receptor and bacteriorhodopsin within bicontinuous cubic lipid phases. 1. Relevance to in meso crystallization of integral membrane proteins in monoolein systems

Power struggles in peptide-amphiphile nanostructures

Membrane Protein Structures in Lipid Bilayers; Small-Angle Neutron Scattering With Contrast-Matched Bicontinuous Cubic Phases

Self-assembly and applications of biomimetic and bioactive peptide-amphiphiles

Biomimetic Hierarchical Superstructures: Approaches Using Bicontinuous Microemulsions and Electrodeposition

Self-assembly of amphiphilic peptides

Structure-Function Relationships of the Neisserial EptA Enzyme Responsible for Phosphoethanolamine Decoration of Lipid A: Rationale for Drug Targeting

Regulatory Landscape of the Pseudomonas aeruginosa Phosphoethanolamine Transferase Gene eptA in the Context of Colistin Resistance.

Direct demonstration of lipid phosphorylation in the lipid bilayer of the biomimetic bicontinuous cubic phase using the confined enzyme lipid A phosphoethanolamine transferase