A5039507161- Lipid Membrane Structure and Behavior
- Force Microscopy Techniques and Applications
- RNA and protein synthesis mechanisms
- Mass Spectrometry Techniques and Applications
- Advanced Electron Microscopy Techniques and Applications
- Photoreceptor and optogenetics research
- Adipose Tissue and Metabolism
- Mitochondrial Function and Pathology
- Photosynthetic Processes and Mechanisms
- Molecular Junctions and Nanostructures
- Advanced biosensing and bioanalysis techniques
- Protein Structure and Dynamics
- Bacterial Genetics and Biotechnology
- Molecular Sensors and Ion Detection
- Muscle metabolism and nutrition
- Ion channel regulation and function
- Advanced NMR Techniques and Applications
- Supramolecular Self-Assembly in Materials
- thermodynamics and calorimetric analyses
- Bacteriophages and microbial interactions
- Polymer Surface Interaction Studies
- Electron and X-Ray Spectroscopy Techniques
- NMR spectroscopy and applications
- Hemoglobin structure and function
- Nanopore and Nanochannel Transport Studies
Centre National de la Recherche Scientifique
2011-2024
Institut de Biologie Physico-Chimique
2012-2024
Université Paris Cité
2011-2024
Laboratoire de Biologie Physico-Chimique des Protéines Membranaires
2009-2023
Sorbonne Université
2005-2015
Délégation Paris 7
2011-2014
Yale University
2006-2008
Service de Physique de l'État Condensé
2007
Université d'Avignon et des Pays de Vaucluse
2007
CEA Paris-Saclay
2007
Amphipols (APols) are short amphipathic polymers that can substitute for detergents to keep integral membrane proteins (MPs) water soluble. In this review, we discuss their structure and solution behavior; the way they associate with MPs; structure, dynamics, properties of resulting complexes. All MPs tested date form water-soluble complexes APols, biochemical stability is in general greatly improved compared detergent solutions. The functionality ligand-binding APol-trapped reviewed,...
The extraction of membrane proteins from their native environment by detergents is central to biophysical characterization. Recent studies have emphasized that may perturb the structure locally and modify dynamics proteins. However, it remains challenging determine whether these perturbations are negligible or could be responsible for misfolded conformations, altering protein's function. In this work, we propose an original strategy combining functional molecular simulations address...
One of the major obstacles to membrane protein (MP) structural studies is destabilizing effect detergents. Amphipols (APols) are short amphipathic polymers that can substitute for detergents keep MPs water-soluble under mild conditions. In present work, we have explored feasibility studying structure APol-complexed by NMR. As a test MP, chose 171-residue transmembrane domain outer MP A from Escherichia coli (tOmpA), whose x-ray and NMR structures in detergent known. 2 H, 15 N-labeled tOmpA...
Amphipols (APols) are short amphipathic polymers that can substitute for detergents to keep membrane proteins (MPs) water-soluble while stabilizing them biochemically. We have examined the factors determine size and dispersity of MP/APol complexes studied dynamics association, taking as a model system transmembrane domain Escherichia coli outer protein A (tOmpA) trapped by A8-35, polyacrylate-based APol. Molecular sieving indicates solution properties APol largely those tOmpA/APol complexes....
Membrane proteins (MPs) need to be extracted from biological membranes and purified in their native state for most structural functional vitro investigations. Amphiphilic copolymers, such as amphipols (APols), have emerged very useful alternatives detergents keeping MPs water-soluble under form. However, classical APols, poly(acrylic acid) (PAA) derivatives, seldom enable direct MP extraction. Poly(styrene maleic anhydride) copolymers (SMAs), which bear aromatic rings hydrophobic side...
The translational diffusion coefficient of an integral membrane protein/surfactant complex has been measured using a novel pulsed field gradient NMR method. In this new approach, the information about localization molecules is temporarily stored in form longitudinal magnetization isotopes with long spin−lattice relaxation times. This allows one to increase duration interval by 1 order magnitude. Unlike standard proton methods gradients and stimulated echoes, method can be applied...
Over the past decade, structural biology of membrane proteins (MPs) has taken a new turn thanks to epoch-making technical progress in single-particle electron cryo-microscopy (cryo-EM) as well improvements sample preparation. The present analysis provides an overview extent and modes usage various types surfactants for cryo-EM studies. Digitonin, dodecylmaltoside, protein-based nanodiscs, lauryl maltoside-neopentyl glycol, glyco-diosgenin, amphipols (APols) are most popular at vitrification...
The aggregation of integral membrane proteins (IMPs) in aqueous media is a significant concern for mechanistic investigations and pharmaceutical applications this important class proteins. Complexation IMPs with amphiphiles, either detergents or short amphiphilic polymers known as amphipols (APols), renders water-soluble. It common knowledge that IMP−detergent complexes are labile, while IMP−APol exceptionally stable do not dissociate even under conditions extreme dilution. To understand the...
Whether for fundamental biological research or diagnostic and drug discovery applications, protein micro- nanoarrays are attractive technologies because of their low sample consumption, high-throughput, multiplexing capabilities. However, the arraying platforms developed so far still not able to handle membrane proteins, specific methods selectively immobilize these hydrophobic fragile molecules needed understand function structural complexity. Here we integrate two technologies,...
Amphipols (APols) are short amphipathic polymers that stabilize membrane proteins (MPs) in aqueous solutions. In the present study, A8-35, a polyacrylate-based APol, was grafted with hexahistidine tags (His6-tags). The synthesis and characterization of this novel functionalized named HistAPol, described. Its ability to immobilize MPs on nickel ion-bearing surfaces tested using two complementary methods, immobilized metal affinity chromatography (IMAC) surface plasmon resonance (SPR)....
Amphipols (APols) are specially designed amphipathic polymers that stabilize membrane proteins (MPs) in aqueous solutions the absence of detergent. A8–35, a polyacrylate-based APol, has been grafted with an oligodeoxynucleotide (ODN). The synthesis, purification and properties resulting 'OligAPol' have investigated. Grafting was performed by reacting ODN carrying amine-terminated arm carboxylates A8–35. use OligAPol for trapping MPs immobilizing them onto solid supports tested using...
Membrane proteins (MPs) are essential for numerous important biological processes. Recently, mass spectrometry (MS), coupled with an array of related techniques, has been used to probe the structural properties MPs and their complexes. Typically, detergent micelles have employed delivering into gas-phase, but these complexes intrinsic that can limit utility studies using MS methods. Amphipols (APols) advantages over shown be capable native gas-phase. Comparing six different APols which vary...
Abstract Membrane proteins are essential for cellular growth, signalling and homeostasis, making up a large proportion of therapeutic targets. However, the necessity solubilising agent to extract them from membrane creates challenges in their structural functional study. Although amphipols have been very effective single-particle electron cryo-microscopy (cryoEM) mass spectrometry, they rely on initial detergent extraction before exchange into amphipol environment. Therefore, circumventing...