Tribet, C. published the artcileThermodynamic Characterization of the Exchange of Detergents and Amphipols at the Surfaces of Integral Membrane Proteins, Quality Control of 85618-21-9, the publication is Langmuir (2009), 25(21), 12623-12634, database is CAplus and MEDLINE.
The aggregation of integral membrane proteins (IMPs) in aqueous media is a significant concern for mechanistic investigations and pharmaceutical applications of this important class of proteins. Complexation of IMPs with amphiphiles, either detergents or short amphiphilic polymers known as amphipols (APols), renders IMPs water-soluble It is common knowledge that IMP-detergent complexes are labile, while IMP-APol complexes are exceptionally stable and do not dissociate even under conditions of extreme dilution To understand the thermodn. origin of this difference in stability and to guide the design of new APols, the authors have studied by isothermal titration calorimetry (ITC) the heat exchanges during two reciprocal processes, the “trapping” of detergent-solubilized IMPs in APols and the “stripping” of IMP-APol complexes by detergents, using two IMPs (the transmembrane domain of porin OmpA from Escherichia coli and bacteriorhodopsin from Halobacterium salinarium), two APols [an anionic polymer derived from acrylic acid (A8-35) and a cationic phosphorylcholine-based polymer (C22-43)], and two neutral detergents [n-octyl thioglucoside (OTG) and n-octyltetraethylene glycol (C8E4)]. In the presence of detergent, free APols and IMP-APol complexes form mixed particles, APol-detergent and IMP-APol-detergent, resp., according to the regular mixing model. Diluting IMP-APol-detergent complexes below the critical micellar concentration (CMC) of the detergent triggers the dispersion of detergent mols. as monomers, a process characterized by an enthalpy of demicellization. The enthalpy of APol ↔ detergent exchange on the hydrophobic surface of IMPs is negligibly small, an indication of the similarity of the mol. interactions of IMPs with the two types of amphiphiles. The enhanced stability against dilution of IMP-APol complexes, compared to IMP-detergent ones, originates from the difference in entropy gain achieved upon release in water of a few APol mols. (in the case of IMP-APol complexes) or several hundred detergent mols. (in the case of IMP-detergent complexes). The data account both for the stability of IMP-APols complexes in the absence of detergent and for the ease with which detergents displace APols from the surface of proteins.
Langmuir published new progress about 85618-21-9. 85618-21-9 belongs to alcohols-buliding-blocks, auxiliary class Tetrahydropyran,Chiral,sulfides,Alcohol, name is (2R,3S,4S,5R,6S)-2-(Hydroxymethyl)-6-(octylthio)tetrahydro-2H-pyran-3,4,5-triol, and the molecular formula is C18H34N4O5S, Quality Control of 85618-21-9.
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