Table 9.1 (continued)
9.30
Transient receptor potential
melastatin-1 (TRPM1)
(~360 kDa)
A8-35
Determination of the oligomeric state of TRPM1/A8-35
complexes prior to EM.
Agosto et al
(2014)
9.31
OmpF trimer (~111 kDa)
A8-35
Examination of the association state of OmpF in the presence
or absence of free A8-35, lipopolysaccharide, and/or EDTA
prior to negative-stain EM studies.
Arunmanee et al.
(2014)
9.32
BR and two GPCRs, the
melanocortin-2 and 4
receptors (~27, ~34 and
~36 kDa, respectively)
A8-35
Determination of the size and homogeneity and purification
of MP/APol complexes following refolding in A8-35 and
prior to NMR studies.
Elter et al. (2014)
9.33
OmpX (~18.6 kDa)
A8-35
Determination of rotational correlation time.
Etzkorn et al.
(2014)
9.34
BLT2 (43.9 kDa)
A8-35 and
perdeuterated
A8-35
(perDAPol)
Comparison of the size and dispersity of BLT2/APol complexes formed using either unlabeled or perdeuterated A8-35.
Giusti et al. (2014)
9.35
P-glycoprotein (PgP)
(~170 kDa)
SMA
Characterization of PgP/SMALP complexes prior to cryoEM.
Gulati et al. (2014)
9.36
Lysophosphatidic acid
receptor 2 (LPA2; fusion
protein)
Poly-γ-glutamic
acid grafted
with octylamine
and glucosamine (APG)
In the frame of characterizing APG for use as an APol,
LPA2/APG complexes were studied by SEC and AFM.
Han et al. (2014)
9.37
BR (~27 kDa)
gonucleotidetagged A8-35
(OligAPol)
Comparison of A8-35- and OligAPol-trapped BR, binding of
and immobilization via a complementary oligonucleotide.
Le Bon et al.
(2014a)
9.38
Light-harvesting complexes II (LHCII) (~75 kDa)
A8-35, NAPol
Comparison of DDM-solubilized and A8-35- or NAPol-trapped complexes.
Opačić et al.
(2014a)
9.39
Mannitol permease (EII mtl )
(~68 kDa)
A8-35 and fluorescein-labeled
A8-35
(FAPolfluo)
Examination of the size, dispersity, and function of
EII mtl /APol complexes prior to fluorescence quenching
experiments.
Opačić et al.
(2014b)
9.40
BR (~27 kDa)
A8-35
Comparison of the dispersity of BR/A8-35 complexes in the
presence or absence of free APol prior to crystallization by
transfer to a lipid mesophase.
Polovinkin et al.
(2014)
9.41
ExbB/ExbD complexes
(monomers ~26 and
~15 kDa, respectively)
A8-35, DAPol,
FAPolNBD
A broad array of biophysical and biochemical methods was
harnessed to establish the mass, composition, shape, and
organization of ExbB4/ExbD2 and ExbB6/ExbD4 complexes
trapped in A8-35 or in deuterated or fluorescent derivatives
thereof.
Sverzhinsky et al.
(2014)
9.42
MexB and OprM from
Pseudomonas aeruginosa,
BR, cytochrome bc1
Biotinylated
A8-35 and
NAPol
Selection of αRep binders targeting MexB and other MPs.
Ferrandez et al.
(2014)
9.43
tOmpA
(~19 kDa)
A8-35 and
polyhistidinetagged A8-35
(HistAPol)
Comparison of the solution behavior of tOmpA/A8-35 and
tOmpA/HistAPol complexes prior to immobilization studies.
Giusti et al. (2015)
9.44
Human adenosine A2A
receptor (A2AR) (44.7 kDa)
SMA
Examination of the solution properties and stability of
SMALP-trapped A2AR
Jamshad et al.
(2015)
9.45
Insulin-responsive facilitative glucose transporter
GLUT4 (~43 kDa)
A8-35
GLUT4 overexpressed in HEK-293 cells was purified in
LMNG and transferred to nanodiscs, A8-35, or proteoliposomes. GLUT4/A8-35 complexes were studied by SEC, denaturation and renaturation studies, and ligand binding.
Kraft et al. (2015)
9.46
Transient receptor potential
ankyrin 1 channel (TRPA1)
(~525 kDa)
PMAL-C8
Characterization of TRPA1/PMAL-C8 complexes prior to
cryo-EM.
Paulsen et al.
(2015)
9.47
Multidrug transporter AcrB
trimer (~360 kDa)
SMA
Examination as a function of ionic strength of the tendency of
SMALP-trapped AcrB trimers to form SMALP-mediated
"doublets".
Postis et al. (2015)
9.48
Human transient receptor
potential melastatin 4
channel (TRPM4)
(668 kDa; fusion protein)
A8-35
In the frame of a broad study of the oligomeric state of
TRPM4, the dispersity of TRPM4/A8-35 complexes is examined by SEC.
Constantine et al.
(2016)
9.49
BR (~27 kDa)
SMA, SMA-SH
SEC is used to compare the size of the particles formed upon
extracting BR from proteoliposomes either with SMA or with
a thiolated version thereof (SMA-SH).
Lindhoud et al.
(2016)
9.50
Melatonin MT1R
(~39 kDa) and ghrelin
GHS-R1a (~41 kDa)
receptors
SMA
CHS-R1a was expressed in inclusion bodies, folded in
A8-35, and transferred to lipid vesicles. MT1R was expressed
in Chinese hamster ovary (CHO) cells, from which
membrane fragments were purified. The two GPCRs were
extracted with SMA and the particles characterized by SEC.
Logez et al. (2016)
9.51
Polycystic Kidney Disease
Channel-2 (PKD2)
(~325 kDa)
A8-35
In the frame of a cryo-EM study, the size and distribution of
PKD2/A8-35 and PKD2/nanodisc complexes are compared
by SEC.
Shen et al. (2016)
9.52
Mitochondrial respirasome
(I1III2IV1 supercomplex)
(~1.7 MDa)
A8-35
A8-35-trapped mitochondrial complexes and supercomplexes
are analyzed by BN-PAGE, SGSV, and spectroscopic approaches.
Shinzawa-Itoh et
al. (2016)
9.53
Mitochondrial respirasome
(I1III2IV1 supercomplex)
(~1.7 MDa)
A8-35
In the context of a cryo-EM study, respirasome/A8-35
complexes are examined by BN-PAGE.
Sousa et al. (2016)
9.54
Dimeric mitochondrial
ATP-synthase from Polytomella sp. (~1.6 MDa)
A8-35
High concentrations of A8-35 (up to 3.5%) are used to disrupt the F1FO ATP-synthase into subcomplexes, which are
analyzed by BN-PAGE and 2D gels.
Vázquez-Acevedo
et al. (2016)
9.55
Bacteriorhodopsin from
Haloquadratum walsbyi
(HwBR) (~27 kDa)
SMA
HwBR/SMA complexes were characterized by SEC, DLS,
and UV-visible spectroscopy before being delivered to a
lipidic mesophase for crystallization.
Broecker et al.
(2017)
9.56
Lysophosphatidic acid
receptor 2 (LPA2; fusion
protein)
Poly-γ-glutamic
acid grafted
with octylamine,
glucosamine,
and diethyl
aminopropylamine
At variance with the SEC profile shown in Study 9.36, that
shown here seems to indicate that the complexes formed by
LPA2 and a variant of APG elute mostly in the void volume
Han et al. (2017)
of the column, suggesting that they are very large or aggregated.
9.57
Transient receptor potential
(TRP) channel NOMPC
(~760 kDa) from Drosophila melanogaster.
A8-35
In the frame of a cryo-EM study, a comparative SEC analysis
is presented of A8-35- and ND-trapped NOMPC.
Jin et al. (2017)
9.58
E. coli outer membrane
phospholipase A (OmpLA)
(~31 kDa)
Alternating
diisobutylene/
maleic acid
copolymer
(DIBMA)
SEC and DLS profiles of OmpLA/DIBMA particles.
Oluwole et al.
(2017)
Study
Membrane proteins
(MW)
Amphipol
SANS
SAXS
SGSV
AUC
SEC
DLS
BNPAGE
Comments
References
Abbreviations: AFM atomic force microscopy, APG poly-γ-glutamic acid grafted with octylamine
and glucosamine, AUC analytical ultracentrifugation, BN-PAGE Blue-Native polyacrylamide gel electrophoresis, cryo-EM electron cryomicroscopy, DIBMA alternating diisobutylene/maleic acid copolymer,
9.30
Transient receptor potential
melastatin-1 (TRPM1)
(~360 kDa)
A8-35
Determination of the oligomeric state of TRPM1/A8-35
complexes prior to EM.
Agosto et al
(2014)
9.31
OmpF trimer (~111 kDa)
A8-35
Examination of the association state of OmpF in the presence
or absence of free A8-35, lipopolysaccharide, and/or EDTA
prior to negative-stain EM studies.
Arunmanee et al.
(2014)
9.32
BR and two GPCRs, the
melanocortin-2 and 4
receptors (~27, ~34 and
~36 kDa, respectively)
A8-35
Determination of the size and homogeneity and purification
of MP/APol complexes following refolding in A8-35 and
prior to NMR studies.
Elter et al. (2014)
9.33
OmpX (~18.6 kDa)
A8-35
Determination of rotational correlation time.
Etzkorn et al.
(2014)
9.34
BLT2 (43.9 kDa)
A8-35 and
perdeuterated
A8-35
(perDAPol)
Comparison of the size and dispersity of BLT2/APol complexes formed using either unlabeled or perdeuterated A8-35.
Giusti et al. (2014)
9.35
P-glycoprotein (PgP)
(~170 kDa)
SMA
Characterization of PgP/SMALP complexes prior to cryoEM.
Gulati et al. (2014)
9.36
Lysophosphatidic acid
receptor 2 (LPA2; fusion
protein)
Poly-γ-glutamic
acid grafted
with octylamine
and glucosamine (APG)
In the frame of characterizing APG for use as an APol,
LPA2/APG complexes were studied by SEC and AFM.
Han et al. (2014)
9.37
BR (~27 kDa)
gonucleotidetagged A8-35
(OligAPol)
Comparison of A8-35- and OligAPol-trapped BR, binding of
and immobilization via a complementary oligonucleotide.
Le Bon et al.
(2014a)
9.38
Light-harvesting complexes II (LHCII) (~75 kDa)
A8-35, NAPol
Comparison of DDM-solubilized and A8-35- or NAPol-trapped complexes.
Opačić et al.
(2014a)
9.39
Mannitol permease (EII mtl )
(~68 kDa)
A8-35 and fluorescein-labeled
A8-35
(FAPolfluo)
Examination of the size, dispersity, and function of
EII mtl /APol complexes prior to fluorescence quenching
experiments.
Opačić et al.
(2014b)
9.40
BR (~27 kDa)
A8-35
Comparison of the dispersity of BR/A8-35 complexes in the
presence or absence of free APol prior to crystallization by
transfer to a lipid mesophase.
Polovinkin et al.
(2014)
9.41
ExbB/ExbD complexes
(monomers ~26 and
~15 kDa, respectively)
A8-35, DAPol,
FAPolNBD
A broad array of biophysical and biochemical methods was
harnessed to establish the mass, composition, shape, and
organization of ExbB4/ExbD2 and ExbB6/ExbD4 complexes
trapped in A8-35 or in deuterated or fluorescent derivatives
thereof.
Sverzhinsky et al.
(2014)
9.42
MexB and OprM from
Pseudomonas aeruginosa,
BR, cytochrome bc1
Biotinylated
A8-35 and
NAPol
Selection of αRep binders targeting MexB and other MPs.
Ferrandez et al.
(2014)
9.43
tOmpA
(~19 kDa)
A8-35 and
polyhistidinetagged A8-35
(HistAPol)
Comparison of the solution behavior of tOmpA/A8-35 and
tOmpA/HistAPol complexes prior to immobilization studies.
Giusti et al. (2015)
9.44
Human adenosine A2A
receptor (A2AR) (44.7 kDa)
SMA
Examination of the solution properties and stability of
SMALP-trapped A2AR
Jamshad et al.
(2015)
9.45
Insulin-responsive facilitative glucose transporter
GLUT4 (~43 kDa)
A8-35
GLUT4 overexpressed in HEK-293 cells was purified in
LMNG and transferred to nanodiscs, A8-35, or proteoliposomes. GLUT4/A8-35 complexes were studied by SEC, denaturation and renaturation studies, and ligand binding.
Kraft et al. (2015)
9.46
Transient receptor potential
ankyrin 1 channel (TRPA1)
(~525 kDa)
PMAL-C8
Characterization of TRPA1/PMAL-C8 complexes prior to
cryo-EM.
Paulsen et al.
(2015)
9.47
Multidrug transporter AcrB
trimer (~360 kDa)
SMA
Examination as a function of ionic strength of the tendency of
SMALP-trapped AcrB trimers to form SMALP-mediated
"doublets".
Postis et al. (2015)
9.48
Human transient receptor
potential melastatin 4
channel (TRPM4)
(668 kDa; fusion protein)
A8-35
In the frame of a broad study of the oligomeric state of
TRPM4, the dispersity of TRPM4/A8-35 complexes is examined by SEC.
Constantine et al.
(2016)
9.49
BR (~27 kDa)
SMA, SMA-SH
SEC is used to compare the size of the particles formed upon
extracting BR from proteoliposomes either with SMA or with
a thiolated version thereof (SMA-SH).
Lindhoud et al.
(2016)
9.50
Melatonin MT1R
(~39 kDa) and ghrelin
GHS-R1a (~41 kDa)
receptors
SMA
CHS-R1a was expressed in inclusion bodies, folded in
A8-35, and transferred to lipid vesicles. MT1R was expressed
in Chinese hamster ovary (CHO) cells, from which
membrane fragments were purified. The two GPCRs were
extracted with SMA and the particles characterized by SEC.
Logez et al. (2016)
9.51
Polycystic Kidney Disease
Channel-2 (PKD2)
(~325 kDa)
A8-35
In the frame of a cryo-EM study, the size and distribution of
PKD2/A8-35 and PKD2/nanodisc complexes are compared
by SEC.
Shen et al. (2016)
9.52
Mitochondrial respirasome
(I1III2IV1 supercomplex)
(~1.7 MDa)
A8-35
A8-35-trapped mitochondrial complexes and supercomplexes
are analyzed by BN-PAGE, SGSV, and spectroscopic approaches.
Shinzawa-Itoh et
al. (2016)
9.53
Mitochondrial respirasome
(I1III2IV1 supercomplex)
(~1.7 MDa)
A8-35
In the context of a cryo-EM study, respirasome/A8-35
complexes are examined by BN-PAGE.
Sousa et al. (2016)
9.54
Dimeric mitochondrial
ATP-synthase from Polytomella sp. (~1.6 MDa)
A8-35
High concentrations of A8-35 (up to 3.5%) are used to disrupt the F1FO ATP-synthase into subcomplexes, which are
analyzed by BN-PAGE and 2D gels.
Vázquez-Acevedo
et al. (2016)
9.55
Bacteriorhodopsin from
Haloquadratum walsbyi
(HwBR) (~27 kDa)
SMA
HwBR/SMA complexes were characterized by SEC, DLS,
and UV-visible spectroscopy before being delivered to a
lipidic mesophase for crystallization.
Broecker et al.
(2017)
9.56
Lysophosphatidic acid
receptor 2 (LPA2; fusion
protein)
Poly-γ-glutamic
acid grafted
with octylamine,
glucosamine,
and diethyl
aminopropylamine
At variance with the SEC profile shown in Study 9.36, that
shown here seems to indicate that the complexes formed by
LPA2 and a variant of APG elute mostly in the void volume
Han et al. (2017)
of the column, suggesting that they are very large or aggregated.
9.57
Transient receptor potential
(TRP) channel NOMPC
(~760 kDa) from Drosophila melanogaster.
A8-35
In the frame of a cryo-EM study, a comparative SEC analysis
is presented of A8-35- and ND-trapped NOMPC.
Jin et al. (2017)
9.58
E. coli outer membrane
phospholipase A (OmpLA)
(~31 kDa)
Alternating
diisobutylene/
maleic acid
copolymer
(DIBMA)
SEC and DLS profiles of OmpLA/DIBMA particles.
Oluwole et al.
(2017)
Study
Membrane proteins
(MW)
Amphipol
SANS
SAXS
SGSV
AUC
SEC
DLS
BNPAGE
Comments
References
Abbreviations: AFM atomic force microscopy, APG poly-γ-glutamic acid grafted with octylamine
and glucosamine, AUC analytical ultracentrifugation, BN-PAGE Blue-Native polyacrylamide gel electrophoresis, cryo-EM electron cryomicroscopy, DIBMA alternating diisobutylene/maleic acid copolymer,