Membrane proteins in nanotechnology

Curnow, Paul

doi:10.1042/bst0370643

Cited by 12 publications

(7 citation statements)

References 80 publications

(75 reference statements)

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“…As such, IMPs naturally exist within lipid membranes where they make extensive non-polar contacts with the hydrophobic core of the bilayer 6 . The poor water solubility of IMPs creates a roadblock to characterizing their structure and function 7 – 9 , and also represents one of the most substantial barriers to developing membrane protein technologies 10 . To overcome this challenge, IMPs can be solubilized using detergents or detergent-like reagents ( e.g.…”

Section: Introductionmentioning

confidence: 99%

RETRACTED ARTICLE: A water-soluble DsbB variant that catalyzes disulfide-bond formation in vivo

et al. 2017

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Escherichia coli DsbB is a transmembrane enzyme that catalyzes the re-oxidation of the periplasmic oxidase DsbA by ubiquinone. Here, we sought to convert membrane-bound DsbB into a water-soluble biocatalyst by leveraging a previously described method for in vivo solubilization of integral membrane proteins (IMPs). When solubilized DsbB variants were co-expressed with an export-defective copy of DsbA in the cytoplasm of wild-type E. coli cells, artificial oxidation pathways were created that efficiently catalyzed de novo disulfide bond formation in a range of substrate proteins and in a manner that depended on both DsbA and quinone. Hence, DsbB solubilization was achieved with preservation of both catalytic activity and substrate specificity. Moreover, given the generality of the solubilization technique, the results presented here should pave the way for unlocking the biocatalytic potential of other membrane-bound enzymes whose utility has been limited by poor stability of IMPs outside of their native lipid bilayer context.

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Section: Introductionmentioning

confidence: 99%

RETRACTED ARTICLE: A water-soluble DsbB variant that catalyzes disulfide-bond formation in vivo

et al. 2017

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“…[ [89][90][91] • Nano-scale cantilever arrays Microscopic, flexible beams resembling a row of diving boards -are built using semiconductor lithographic techniques. Such micron-sized devices, comprising many nanometer-sized cantilevers constructed as part of a larger diagnostic device, can provide rapid and sensitive high-throughput detection of proteins, DNA, RNA and whole-cell for a broad range of applications ranging from disease diagnosis to analytical chemistry.…”

Section: Magnetic Nanoparticlesmentioning

confidence: 99%

Nanotechnology and Nanomedicine: Going Small Means Aiming Big

Teli

Mutalik

Rajanikant

2010

CPD

146

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Nanotechnology is an emerging branch of science for designing tools and devices of size 1 to 100 nm with specific function at the cellular, atomic and molecular levels. The concept of employing nanotechnology in biomedical research and clinical practice is best known as nanomedicine. Nanomedicine is an upcoming field that could potentially make a major impact to human health. Nanomaterials are increasingly used in diagnostics, imaging and targeted drug delivery. Nanotechnology will assist the integration of diagnostics/imaging with therapeutics and facilitates the development of personalized medicine, i.e. prescription of specific medications best suited for an individual. This review provides an integrated overview of application of nanotechnology based molecular diagnostics and drug delivery in the development of nanomedicine and ultimately personalized medicine. Finally, we identify critical gaps in our knowledge of nanoparticle toxicity and how these gaps need to be evaluated to enable nanotechnology to transit safely from bench to bedside.

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“…[1] Bovine rhodopsin is a canonical prototype of G-protein-coupled receptors (GPCRs), the largest family of membrane proteins (MPs) in the human genome, and the most frequent drug targets. [2] Understanding GPCR activation mechanisms is far reaching in terms of GPCR-based biological signalling, as well pharmaceutical development.…”

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confidence: 99%

A Usual G‐Protein‐Coupled Receptor in Unusual Membranes

et al. 2015

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G-protein-coupled receptors (GPCRs) are the largest family of membrane-bound receptors and constitute ~50% of all known drug targets. They offer great potential for membrane protein nanotechnologies. We report here a charge-interaction-directed reconstitution mechanism that induces spontaneous insertion of bovine rhodopsin, the eukaryotic GPCR, into both lipid- and polymer-based artificial membranes. We reveal a new allosteric mode of rhodopsin activation incurred by the non-biological membranes: the cationic membrane drives a transition from inactive MI to activated MII state in the absence of high [H+] or negative spontaneous curvature. We attribute this activation to the attractive charge interaction between the membrane surface and the deprotonated Glu134 residue of the rhodopsin-conserved ERY sequence motif that helps break the cytoplasmic “ionic lock”. This study unveils a novel design concept of non-biological membranes to reconstitute and harness GPCR functions in synthetic systems.

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Membrane proteins in nanotechnology

Cited by 12 publications

References 80 publications

RETRACTED ARTICLE: A water-soluble DsbB variant that catalyzes disulfide-bond formation in vivo

RETRACTED ARTICLE: A water-soluble DsbB variant that catalyzes disulfide-bond formation in vivo

Nanotechnology and Nanomedicine: Going Small Means Aiming Big

A Usual G‐Protein‐Coupled Receptor in Unusual Membranes

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