Trubetskoy, O.V., Finel, M., Burke, T.J., Trubetskoy, V.S. (2006) Evaluation of synthetic polymeric micelles as a
stabilization medium for the handling of membrane proteins in pharmaceutical drug discovery. J. Pharm.
Pharmaceut. Sci. 9:271–280.
Vargas, C., Cuevas Arenas, R., Frotscher, E., Keller, S. (2015) Nanoparticle self-assembly in mixtures of phospholipids
with styrene/maleic acid copolymers or fluorinated surfactants. Nanoscale 7:20685–20696.
Veregin, R.P.N., Georges, M.K., Kazmaier, P.M., Hamer, G.K. (1993) Free radical polymerizations for narrow
polydispersity resins: electron spin resonance studies of the kinetics and mechanism. Macromolecules 26:5316–5320.
Vial, F., Cousin, F., Bouteiller, L., Tribet, C. (2009) Rate of permeabilization of giant vesicles by amphiphilic
polyacrylates compared to the adsorption of these polymers onto large vesicles and tethered lipid bilayers. Langmuir
25:7506–7513.
Vial, F., Oukhaled, A.G., Auvray, L., Tribet, C. (2007) Long-living channels of well-defined radius opened in lipid
bilayers by polydisperse, hydrophobically-modified polyacrylic acids. Soft Matter 3:75–78.
Vial, F., Rabhi, S., Tribet, C. (2005) Association of octyl-modified poly(acrylic acid) onto unilamellar vesicles of lipids
and kinetics of vesicle disruption. Langmuir 21:853–862.
Volpert, E., Selb, J., Candau, F. (1996) Influence of the hydrophobe structure on composition, microstructure, and
rheology in associating polyacrylamides prepared by micellar copolymerization. Macromolecules 29:1452–1463.
Wagner, H.L. (1987) The Mark–Houwink–Sakurada relation for poly(methyl methacrylate). J. Phys. Chem. Ref. Data
16:165–173.
Wang, J.-S., Matyjaszewski, K. (1995) Controlled “living” radical polymerization. Atom transfer radical polymerization
in the presence of transition-metal complexes. J. Am. Chem. Soc. 117:5614–5615.
Wang, K.T., Iliopoulos, I., Audebert, R. (1988) Viscometric behavior of hydrophobically modified poly(sodium acrylate)
Polym. Bull. 20:577–582.
Watkinson, T.G., Calabrese, A.N., Giusti, F., Zoonens, M., Radford, S.E., Ashcroft, A.E. (2015) Systematic analysis of
the use of amphipathic polymers for studies of outer membrane proteins using mass spectrometry. Int. J. Mass
Spectrom. 391:54–61.
Weidner, S.M., Trimpin, S. (2010) Mass spectrometry of synthetic polymers. Anal. Chem. 82:4811–4829.
Wheatley, M., Charlton, J., Jamshad, M., Routledge, S.J., Bailey, S., La-Borde, P.J., Azam, M.T., Logan, R.T., Bill, R.
M., Dafforn, T.R., Poyner, D.R. (2016) GPCR-styrene maleic acid lipid particles (GPCR-SMALPs): their nature and
potential. Biochem. Soc. Trans. 44:619–623.
Yamamoto, H., Hashidzume, A., Morishima, Y. (2000a) Micellization protocols for amphiphilic polyelectrolytes in
water. How do polymers undergo intrapolymer associations? Polym. J. 32:745–752.
Yamamoto, H., Tomatsu, I., Hashidzume, A., Morishima, Y. (2000b) Associative properties in water of copolymers of
sodium 2-(acrylamido)-2-methylpropanesulfonate and methacrylamides substituted with alkyl groups of varying
lengths. Macromolecules 33:7852–7861.
Yokozawa, T., Yokoyama, A. (2004) Chain-growth polycondensation: living polymerization nature in polycondensation
and approach to condensation polymer architecture. Polym. J. 36:65–83.
Yoshimoto, K., Hirase, T., Nemoto, S., Hatta, T., Nagasaki, Y. (2008) Facile construction of sulfanyl-terminated poly
(ethylene glycol)-brushed layer on a gold surface for protein immobilization by the combined use of sulfanyl-ended
telechelic and semitelechelic poly(ethylene glycol)s. Langmuir 24:9623–9629.
Zaccai, G. (2000) How soft is a protein? A protein dynamics force constant measured by neutron scattering. Science
288:1604–1607.
Zaccai, G. (2011) Neutron scattering perspectives for protein dynamics. J. Non-Cryst. Solids 357:615–621.
Zaccai, G. (2013) The ecology of protein dynamics. Curr. Phys. Chem. 3:9–16.
Zhang, R., Sahu, I.D., Liu, L., Osatuke, A., Comer, R.G., Dabney-Smith, C., Lorigan, G.A. (2015) Characterizing the
structure of lipodisq nanoparticles for membrane protein spectroscopic studies. Biochim. Biophys. Acta
1848:329–333.
Zhao, J., Wang, H., Liu, J., Deng, L., Liu, J., Dong, A., Zhang, J. (2013) Comb-like amphiphilic copolymers bearing
acetal-functionalized backbones with the ability of acid-triggered hydrophobic-to-hydrophilic transition as effective
nanocarriers for intracellular release of curcumin. Biomacromolecules 14:3973–3984.
Zoonens, M., Catoire, L.J., Giusti, F., Popot, J.-L. (2005) NMR study of a membrane protein in detergent-free aqueous
solution. Proc. Natl. Acad. Sci. USA 102:8893–8898.
Zoonens, M., Giusti, F., Zito, F., Popot, J.-L. (2007) Dynamics of membrane protein/amphipol association studied by
Förster resonance energy transfer. Implications for in vitro studies of amphipol-stabilized membrane proteins.
Biochemistry 46:10392–10404.
Zoonens, M., Popot, J.-L. (2014) Amphipols for each season. J. Membr. Biol. 247:759–796.
236
4 Chemical Structure, Synthesis, and Physical-Chemical Properties of Amphipols
stabilization medium for the handling of membrane proteins in pharmaceutical drug discovery. J. Pharm.
Pharmaceut. Sci. 9:271–280.
Vargas, C., Cuevas Arenas, R., Frotscher, E., Keller, S. (2015) Nanoparticle self-assembly in mixtures of phospholipids
with styrene/maleic acid copolymers or fluorinated surfactants. Nanoscale 7:20685–20696.
Veregin, R.P.N., Georges, M.K., Kazmaier, P.M., Hamer, G.K. (1993) Free radical polymerizations for narrow
polydispersity resins: electron spin resonance studies of the kinetics and mechanism. Macromolecules 26:5316–5320.
Vial, F., Cousin, F., Bouteiller, L., Tribet, C. (2009) Rate of permeabilization of giant vesicles by amphiphilic
polyacrylates compared to the adsorption of these polymers onto large vesicles and tethered lipid bilayers. Langmuir
25:7506–7513.
Vial, F., Oukhaled, A.G., Auvray, L., Tribet, C. (2007) Long-living channels of well-defined radius opened in lipid
bilayers by polydisperse, hydrophobically-modified polyacrylic acids. Soft Matter 3:75–78.
Vial, F., Rabhi, S., Tribet, C. (2005) Association of octyl-modified poly(acrylic acid) onto unilamellar vesicles of lipids
and kinetics of vesicle disruption. Langmuir 21:853–862.
Volpert, E., Selb, J., Candau, F. (1996) Influence of the hydrophobe structure on composition, microstructure, and
rheology in associating polyacrylamides prepared by micellar copolymerization. Macromolecules 29:1452–1463.
Wagner, H.L. (1987) The Mark–Houwink–Sakurada relation for poly(methyl methacrylate). J. Phys. Chem. Ref. Data
16:165–173.
Wang, J.-S., Matyjaszewski, K. (1995) Controlled “living” radical polymerization. Atom transfer radical polymerization
in the presence of transition-metal complexes. J. Am. Chem. Soc. 117:5614–5615.
Wang, K.T., Iliopoulos, I., Audebert, R. (1988) Viscometric behavior of hydrophobically modified poly(sodium acrylate)
Polym. Bull. 20:577–582.
Watkinson, T.G., Calabrese, A.N., Giusti, F., Zoonens, M., Radford, S.E., Ashcroft, A.E. (2015) Systematic analysis of
the use of amphipathic polymers for studies of outer membrane proteins using mass spectrometry. Int. J. Mass
Spectrom. 391:54–61.
Weidner, S.M., Trimpin, S. (2010) Mass spectrometry of synthetic polymers. Anal. Chem. 82:4811–4829.
Wheatley, M., Charlton, J., Jamshad, M., Routledge, S.J., Bailey, S., La-Borde, P.J., Azam, M.T., Logan, R.T., Bill, R.
M., Dafforn, T.R., Poyner, D.R. (2016) GPCR-styrene maleic acid lipid particles (GPCR-SMALPs): their nature and
potential. Biochem. Soc. Trans. 44:619–623.
Yamamoto, H., Hashidzume, A., Morishima, Y. (2000a) Micellization protocols for amphiphilic polyelectrolytes in
water. How do polymers undergo intrapolymer associations? Polym. J. 32:745–752.
Yamamoto, H., Tomatsu, I., Hashidzume, A., Morishima, Y. (2000b) Associative properties in water of copolymers of
sodium 2-(acrylamido)-2-methylpropanesulfonate and methacrylamides substituted with alkyl groups of varying
lengths. Macromolecules 33:7852–7861.
Yokozawa, T., Yokoyama, A. (2004) Chain-growth polycondensation: living polymerization nature in polycondensation
and approach to condensation polymer architecture. Polym. J. 36:65–83.
Yoshimoto, K., Hirase, T., Nemoto, S., Hatta, T., Nagasaki, Y. (2008) Facile construction of sulfanyl-terminated poly
(ethylene glycol)-brushed layer on a gold surface for protein immobilization by the combined use of sulfanyl-ended
telechelic and semitelechelic poly(ethylene glycol)s. Langmuir 24:9623–9629.
Zaccai, G. (2000) How soft is a protein? A protein dynamics force constant measured by neutron scattering. Science
288:1604–1607.
Zaccai, G. (2011) Neutron scattering perspectives for protein dynamics. J. Non-Cryst. Solids 357:615–621.
Zaccai, G. (2013) The ecology of protein dynamics. Curr. Phys. Chem. 3:9–16.
Zhang, R., Sahu, I.D., Liu, L., Osatuke, A., Comer, R.G., Dabney-Smith, C., Lorigan, G.A. (2015) Characterizing the
structure of lipodisq nanoparticles for membrane protein spectroscopic studies. Biochim. Biophys. Acta
1848:329–333.
Zhao, J., Wang, H., Liu, J., Deng, L., Liu, J., Dong, A., Zhang, J. (2013) Comb-like amphiphilic copolymers bearing
acetal-functionalized backbones with the ability of acid-triggered hydrophobic-to-hydrophilic transition as effective
nanocarriers for intracellular release of curcumin. Biomacromolecules 14:3973–3984.
Zoonens, M., Catoire, L.J., Giusti, F., Popot, J.-L. (2005) NMR study of a membrane protein in detergent-free aqueous
solution. Proc. Natl. Acad. Sci. USA 102:8893–8898.
Zoonens, M., Giusti, F., Zito, F., Popot, J.-L. (2007) Dynamics of membrane protein/amphipol association studied by
Förster resonance energy transfer. Implications for in vitro studies of amphipol-stabilized membrane proteins.
Biochemistry 46:10392–10404.
Zoonens, M., Popot, J.-L. (2014) Amphipols for each season. J. Membr. Biol. 247:759–796.
236
4 Chemical Structure, Synthesis, and Physical-Chemical Properties of Amphipols