their micelles makes them more apt to retain lipids in a more or less bilayer-like arrangement. Finally, a
whole gamut of chemical detergents are available, remarkable progress having been achieved, in the
past decades, to make them less and less aggressive (Chap. 2). When one’s target MP can stand them,
detergents remain those surfactants with which the smallest complexes can be formed, an important
point in crystallogenesis and an essential one in solution NMR.
The map has to be taken with quite a few grains of salt. First, each class of surfactants is itself
diverse. To take a couple of examples, “chemical detergents,” as mentioned above, comprise a wide
variety of “strong” detergents, like Triton X-100; “mild” detergents, like DDM; and “very mild”
detergents, like maltose-neopentyl glycol (MNG) amphiphiles (see Chap. 2). “Classical amphipols”
comprise both charged and uncharged species, whose mildness differs, and their respective ability to
directly extract MPs has not been properly investigated (Chap. 5). Second, individual MPs exhibit
different sensitivities to various surfactants, so that the map will vary depending on which target MP is
considered. Third, there exists no comprehensive study encompassing a sufficient number of MPs, a
sufficient number of criteria (solubility, stability, functionality, retention of lipids, and so forth), and
the whole set of surfactants. In many cases, data are very sparse. Retention of MP/lipid interactions, for
instance, is seldom directly measured and must be, in many cases, inferred from indirect information,
such as the solubilizing properties of the surfactant and the stabilizing effect of lipids added to
MP/surfactant complexes. The position assigned to a given class of surfactants is therefore based in
part on indirect, piecemeal information. It is to some extent a matter of personal feeling and, therefore,
open to discussion.
References
Abla, M., Durand, G., Breyton, C., Raynal, S., Ebel, C., Pucci, B. (2012) A diglucosylated fluorinated surfactant to
handle integral membrane proteins in aqueous solution. J. Fluor Chem. 134:63–71.
Abla, M., Durand, G., Pucci, B. (2008) Glucose-based surfactants with hydrogenated, fluorinated, or hemifluorinated
tails: synthesis and comparative physical-chemical characterization. J. Org. Chem. 73:8142–8153.
Abla, M., Unger, S., Keller, S., Bonneté, F., Ebel, C., Pucci, B., Breyton, C., Durand, G. (2015) Micellar and biochemical
properties of a propyl-ended fluorinated surfactant designed for membrane-protein study. J. Colloid Interface Sci.
445:127–136.
Agah, S., Faham, S. (2012) Crystallization of membrane proteins in bicelles. Methods Mol. Biol. 914:3–16.
Ahn, V.E., Leyko, P., Alattia, J.-R., Chen, L., Privé, G.G. (2006) Crystal structures of saposins A and C. Protein Sci.
15:1849–1857.
Akkaladevi, N., Mukherjee, S., Katayama, H., Janowiak, B., Patel, D., Gogol, E.P., Pentelute, B.L., Collier, R.J., Fisher,
M.T. (2015) Following Nature’s lead: On the construction of membrane-inserted toxins in lipid bilayer nanodiscs.
J. Membr. Biol. 248:595–607.
Alvarez, F.J., Orelle, C., Huang, Y., Bajaj, R., Everly, R.M., Klug, C., Davidson, A.L. (2015) Full engagement of
liganded maltose-binding protein stabilizes a semi-open ATP-binding cassette dimer in the maltose transporter. Mol.
Microbiol. 98:878–894.
Anantharamaiah, G.M., Brouillette, C.G., Engler, J.A., De Loof, H., Venkatachalapathi, Y.V., Boogaerts, J., Segrest,
J.P. (1990) Role of amphipathic helices in HDL structure/function. Adv. Exp. Med. Biol. 285:131–140.
Anantharamaiah, G.M., Jones, J.L., Brouillette, C.G., Schmidt, C.F., Chung, B.H., Hughes, T.A., Bhown, A.S., Segrest,
J.P. (1985) Studies of synthetic peptide analogs of the amphipathic helix. Structure of complexes with dimyristoyl
phosphatidylcholine. J. Biol. Chem. 260:10248–10255.
Baas, B.J., Denisov, I.G., Sligar, S.G. (2004) Homotropic cooperativity of monomeric cytochrome P450 3A4 in a
nanoscale native bilayer environment. Arch. Biochem. Biophys. 430:218–228.
Banerjee, S., Huber, T., Sakmar, T.P. (2008) Rapid incorporation of functional rhodopsin into nanoscale apolipoproteinbound bilayer (NABB) particles. J. Mol. Biol. 377:1067–1081.
Barrett, P.J., Song, Y., Van Horn, W.D., Hustedt, E.J., Schafer, J.M., Hadziselimovic, A.H., Beel, A.J., Sanders,
C.R. (2012) The amyloid precursor protein has a flexible transmembrane domain and binds cholesterol. Science
336:1168–1171.
References
135
whole gamut of chemical detergents are available, remarkable progress having been achieved, in the
past decades, to make them less and less aggressive (Chap. 2). When one’s target MP can stand them,
detergents remain those surfactants with which the smallest complexes can be formed, an important
point in crystallogenesis and an essential one in solution NMR.
The map has to be taken with quite a few grains of salt. First, each class of surfactants is itself
diverse. To take a couple of examples, “chemical detergents,” as mentioned above, comprise a wide
variety of “strong” detergents, like Triton X-100; “mild” detergents, like DDM; and “very mild”
detergents, like maltose-neopentyl glycol (MNG) amphiphiles (see Chap. 2). “Classical amphipols”
comprise both charged and uncharged species, whose mildness differs, and their respective ability to
directly extract MPs has not been properly investigated (Chap. 5). Second, individual MPs exhibit
different sensitivities to various surfactants, so that the map will vary depending on which target MP is
considered. Third, there exists no comprehensive study encompassing a sufficient number of MPs, a
sufficient number of criteria (solubility, stability, functionality, retention of lipids, and so forth), and
the whole set of surfactants. In many cases, data are very sparse. Retention of MP/lipid interactions, for
instance, is seldom directly measured and must be, in many cases, inferred from indirect information,
such as the solubilizing properties of the surfactant and the stabilizing effect of lipids added to
MP/surfactant complexes. The position assigned to a given class of surfactants is therefore based in
part on indirect, piecemeal information. It is to some extent a matter of personal feeling and, therefore,
open to discussion.
References
Abla, M., Durand, G., Breyton, C., Raynal, S., Ebel, C., Pucci, B. (2012) A diglucosylated fluorinated surfactant to
handle integral membrane proteins in aqueous solution. J. Fluor Chem. 134:63–71.
Abla, M., Durand, G., Pucci, B. (2008) Glucose-based surfactants with hydrogenated, fluorinated, or hemifluorinated
tails: synthesis and comparative physical-chemical characterization. J. Org. Chem. 73:8142–8153.
Abla, M., Unger, S., Keller, S., Bonneté, F., Ebel, C., Pucci, B., Breyton, C., Durand, G. (2015) Micellar and biochemical
properties of a propyl-ended fluorinated surfactant designed for membrane-protein study. J. Colloid Interface Sci.
445:127–136.
Agah, S., Faham, S. (2012) Crystallization of membrane proteins in bicelles. Methods Mol. Biol. 914:3–16.
Ahn, V.E., Leyko, P., Alattia, J.-R., Chen, L., Privé, G.G. (2006) Crystal structures of saposins A and C. Protein Sci.
15:1849–1857.
Akkaladevi, N., Mukherjee, S., Katayama, H., Janowiak, B., Patel, D., Gogol, E.P., Pentelute, B.L., Collier, R.J., Fisher,
M.T. (2015) Following Nature’s lead: On the construction of membrane-inserted toxins in lipid bilayer nanodiscs.
J. Membr. Biol. 248:595–607.
Alvarez, F.J., Orelle, C., Huang, Y., Bajaj, R., Everly, R.M., Klug, C., Davidson, A.L. (2015) Full engagement of
liganded maltose-binding protein stabilizes a semi-open ATP-binding cassette dimer in the maltose transporter. Mol.
Microbiol. 98:878–894.
Anantharamaiah, G.M., Brouillette, C.G., Engler, J.A., De Loof, H., Venkatachalapathi, Y.V., Boogaerts, J., Segrest,
J.P. (1990) Role of amphipathic helices in HDL structure/function. Adv. Exp. Med. Biol. 285:131–140.
Anantharamaiah, G.M., Jones, J.L., Brouillette, C.G., Schmidt, C.F., Chung, B.H., Hughes, T.A., Bhown, A.S., Segrest,
J.P. (1985) Studies of synthetic peptide analogs of the amphipathic helix. Structure of complexes with dimyristoyl
phosphatidylcholine. J. Biol. Chem. 260:10248–10255.
Baas, B.J., Denisov, I.G., Sligar, S.G. (2004) Homotropic cooperativity of monomeric cytochrome P450 3A4 in a
nanoscale native bilayer environment. Arch. Biochem. Biophys. 430:218–228.
Banerjee, S., Huber, T., Sakmar, T.P. (2008) Rapid incorporation of functional rhodopsin into nanoscale apolipoproteinbound bilayer (NABB) particles. J. Mol. Biol. 377:1067–1081.
Barrett, P.J., Song, Y., Van Horn, W.D., Hustedt, E.J., Schafer, J.M., Hadziselimovic, A.H., Beel, A.J., Sanders,
C.R. (2012) The amyloid precursor protein has a flexible transmembrane domain and binds cholesterol. Science
336:1168–1171.
References
135