Amphipols
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Amphipols
Amphipols (a portmanteau of amphiphilic polymers) are a class of amphiphilic polymers designed to keep membrane proteins soluble in water without the need for detergents, which are traditionally used to this end but tend to be denaturing. Amphipols adsorb onto the hydrophobic transmembrane surface of membrane proteins thanks to their hydrophobic moieties and keep the complexes thus formed water-soluble thanks to the hydrophilic ones. Amphipol-trapped membrane proteins are, as a rule, much more stable than detergent-solubilized ones, which facilitates their study by most biochemical and biophysical approaches. Amphipols can be used to fold denatured membrane proteins to their native form and have proven particularly precious in the field of single-particle electron cryo-microscopy (cryo-EM; see ''e.g.'' ).The properties and uses of amphipols and other non-conventional surfactants are the subject of a book by Jean-Luc Popot.Popot, J.-L. (2018) Membrane proteins in aqueous solutions. ...
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Nanodisc
A nanodisc is a synthetic model membrane system which assists in the study of membrane proteins. Nanodiscs are discoidal proteins in which a lipid bilayer is surrounded by molecules that are amphipathic molecules including proteins, peptides, and synthetic polymers. It is composed of a lipid bilayer of phospholipids with the hydrophobic edge screened by two amphipathic proteins. These proteins are called membrane scaffolding proteins (MSP) and align in double belt formation. Nanodiscs are structurally very similar to discoidal high-density lipoproteins (HDL) and the MSPs are modified versions of apolipoprotein A1 (apoA1), the main constituent in HDL. Nanodiscs are useful in the study of membrane proteins because they can solubilise and stabilise membrane proteins and represent a more native environment than liposomes, detergent micelles, bicelles and amphipols. The art of making nanodiscs has progressed past using only the MSPs and lipids to make particles, leading to alternat ...
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Peptitergents
Peptitergents (a portmanteau of peptide and detergent) are synthetic peptides designed to be lipophilic on one side and hydrophilic on the other upon folding to an α-helical conformation and were designed to solubilize integral membrane proteins in aqueous solution. They can be considered a sub-class of amphipols and are based on earlier fundamental explorations of amphiphilic secondary structures See also * Amphipols Amphipols (a portmanteau of amphiphilic polymers) are a class of amphiphilic polymers designed to keep membrane proteins soluble in water without the need for detergents, which are traditionally used to this end but tend to be denaturing. Amphipol ... References Zwitterionic surfactants {{organic-compound-stub ...
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Portmanteau
A portmanteau word, or portmanteau (, ) is a blend of wordsGarner's Modern American Usage
, p. 644.
in which parts of multiple words are combined into a new word, as in ''smog'', coined by blending ''smoke'' and ''fog'', or ''motel'', from ''motor'' and ''hotel''. In , a portmanteau is a single morph that is analyzed as representing two (or more) underlying morphemes. When portmanteaus shorten established
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Amphiphilic
An amphiphile (from the Greek αμφις amphis, both, and φιλíα philia, love, friendship), or amphipath, is a chemical compound possessing both hydrophilic (''water-loving'', polar) and lipophilic (''fat-loving'') properties. Such a compound is called amphiphilic or amphipathic. Common amphiphilic substances are soaps, detergents, and lipoproteins. The phospholipid amphiphiles are the major structural component of cell membranes. Amphiphiles are the basis for a number of areas of research in chemistry and biochemistry, notably that of lipid polymorphism. Organic compounds containing hydrophilic groups at both ends of the molecule are called bolaamphiphilic. The micelles they form in the aggregate are prolate. Structure The lipophilic group is typically a large hydrocarbon moiety, such as a long chain of the form CH3(CH2)n, with n > 4. The hydrophilic group falls into one of the following categories: # charged groups #* anionic. Examples, with the lipophilic part ...
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Polymers
A polymer (; Greek '' poly-'', "many" + ''-mer'', "part") is a substance or material consisting of very large molecules called macromolecules, composed of many repeating subunits. Due to their broad spectrum of properties, both synthetic and natural polymers play essential and ubiquitous roles in everyday life. Polymers range from familiar synthetic plastics such as polystyrene to natural biopolymers such as DNA and proteins that are fundamental to biological structure and function. Polymers, both natural and synthetic, are created via polymerization of many small molecules, known as monomers. Their consequently large molecular mass, relative to small molecule compounds, produces unique physical properties including toughness, high elasticity, viscoelasticity, and a tendency to form amorphous and semicrystalline structures rather than crystals. The term "polymer" derives from the Greek word πολύς (''polus'', meaning "many, much") and μέρος (''meros'', meani ...
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Membrane Protein
Membrane proteins are common proteins that are part of, or interact with, biological membranes. Membrane proteins fall into several broad categories depending on their location. Integral membrane proteins are a permanent part of a cell membrane and can either penetrate the membrane (transmembrane) or associate with one or the other side of a membrane ( integral monotopic). Peripheral membrane proteins are transiently associated with the cell membrane. Membrane proteins are common, and medically important—about a third of all human proteins are membrane proteins, and these are targets for more than half of all drugs. Nonetheless, compared to other classes of proteins, determining membrane protein structures remains a challenge in large part due to the difficulty in establishing experimental conditions that can preserve the correct conformation of the protein in isolation from its native environment. Function Membrane proteins perform a variety of functions vital to the sur ...
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Cryo-EM
Cryogenic electron microscopy (cryo-EM) is a cryomicroscopy technique applied on samples cooled to cryogenic temperatures. For biological specimens, the structure is preserved by embedding in an environment of vitreous ice. An aqueous sample solution is applied to a grid-mesh and plunge-frozen in liquid ethane or a mixture of liquid ethane and propane. While development of the technique began in the 1970s, recent advances in detector technology and software algorithms have allowed for the determination of biomolecular structures at near-atomic resolution. This has attracted wide attention to the approach as an alternative to X-ray crystallography or NMR spectroscopy for macromolecular structure determination without the need for crystallization. In 2017, the Nobel Prize in Chemistry was awarded to Jacques Dubochet, Joachim Frank, and Richard Henderson "for developing cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution." '' Natu ...
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