Biomimetic triblock copolymer membrane arrays: A stable template for functional membrane proteins
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Biomimetic triblock copolymer membrane arrays : A stable template for functional membrane proteins. / González-Pérez, Alfredo; Stibius, Karin B.; Vissing, Thomas; Nielsen, Claus H.; Mouritsen, Ole G.
In: Langmuir, Vol. 25, No. 18, 15.09.2009, p. 10447-10450.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Biomimetic triblock copolymer membrane arrays
T2 - A stable template for functional membrane proteins
AU - González-Pérez, Alfredo
AU - Stibius, Karin B.
AU - Vissing, Thomas
AU - Nielsen, Claus H.
AU - Mouritsen, Ole G.
PY - 2009/9/15
Y1 - 2009/9/15
N2 - It is demonstrated that biomimetic stable triblock copolymer membrane arrays can be prepared using a scaffold containing 64 apertures of 300 μm diameter each. The membranes were made from a stock solution of block copolymers with decane as a solvent using a new deposition method. By using decane, we avoid low molecular weight solvents such as chloroform and toluene, which are strong protein denaturants. The membranes show a low ionic conductance and a long lifetime at room temperature. Contrast phase microscopy shows the presence of a polymer region delimited by a Plateau-Gibbs border similar to what is observed in black lipid membranes. The ion-channel gramicidin A was successfully incorporated into the membrane in a functional form.
AB - It is demonstrated that biomimetic stable triblock copolymer membrane arrays can be prepared using a scaffold containing 64 apertures of 300 μm diameter each. The membranes were made from a stock solution of block copolymers with decane as a solvent using a new deposition method. By using decane, we avoid low molecular weight solvents such as chloroform and toluene, which are strong protein denaturants. The membranes show a low ionic conductance and a long lifetime at room temperature. Contrast phase microscopy shows the presence of a polymer region delimited by a Plateau-Gibbs border similar to what is observed in black lipid membranes. The ion-channel gramicidin A was successfully incorporated into the membrane in a functional form.
UR - http://www.scopus.com/inward/record.url?scp=70349929812&partnerID=8YFLogxK
U2 - 10.1021/la902417m
DO - 10.1021/la902417m
M3 - Journal article
C2 - 19735126
AN - SCOPUS:70349929812
VL - 25
SP - 10447
EP - 10450
JO - Langmuir
JF - Langmuir
SN - 0743-7463
IS - 18
ER -
ID: 230976831