Structure of Diisobutylene Maleic Acid Copolymer (DIBMA) and Its Lipid Particle as a “Stealth” Membrane-Mimetic for Membrane Protein Research

Author(s):  
Rong Guo ◽  
Jacob Sumner ◽  
Shuo Qian
2020 ◽  
Author(s):  
Rong Guo ◽  
Jacob Sumner ◽  
Shuo Qian

Diisobutylene maleic acid (DIBMA) has been shown to solubilize and purify membrane proteins from a native lipid bilayer into nanodiscs without the need for a detergent. To explore DIBMA lipid particles as a suitable membrane mimetic system for neutron scattering studies of membrane proteins, we measured and determined the contrast matching point of DIBMA to be ~12% (v/v) D2O—similar to that of most protiated lipid molecules, but distinct from that of regular protiated proteins, providing a natural contrast for separating neutron scattering signals. Using SANS contrast variation, we demonstrated that the scattering from the whole lipid particle can be annihilated. Further, the lipid part of the particle shows a well-defined discoidal shape with DIBMA contrast matched. These results demonstrate that the DIBMA lipid particle is an outstanding “stealth” membrane mimetic for membrane proteins.<br>


2020 ◽  
Author(s):  
Rong Guo ◽  
Jacob Sumner ◽  
Shuo Qian

Diisobutylene maleic acid (DIBMA) has been shown to solubilize and purify membrane proteins from a native lipid bilayer into nanodiscs without the need for a detergent. To explore DIBMA lipid particles as a suitable membrane mimetic system for neutron scattering studies of membrane proteins, we measured and determined the contrast matching point of DIBMA to be ~12% (v/v) D2O—similar to that of most protiated lipid molecules, but distinct from that of regular protiated proteins, providing a natural contrast for separating neutron scattering signals. Using SANS contrast variation, we demonstrated that the scattering from the whole lipid particle can be annihilated. Further, the lipid part of the particle shows a well-defined discoidal shape with DIBMA contrast matched. These results demonstrate that the DIBMA lipid particle is an outstanding “stealth” membrane mimetic for membrane proteins.<br>


Author(s):  
Stephanie G. Pitch ◽  
Weekie Yao ◽  
Istvan Szundi ◽  
Jonathan Fay ◽  
Eefei Chen ◽  
...  

2020 ◽  
Author(s):  
Marta Barniol-Xicota ◽  
Steven Verhelst

Membrane proteins are key in a large number of physiological and pathological processes. Their study often involves a prior detergent solubilization step, which strips away the membrane and can jeopardize membrane protein integrity. A recent alternative to detergents encompasses maleic acid based copolymers (xMAs), which disrupt the lipid bilayer and form lipid protein nanodiscs (xMALPs) soluble in aqueous buffer. Although xMALPs are often referred to as native nanodiscs, little is known about the resemblance of their lipid and protein content to the native bilayer. Here we have analyzed prokaryotic and eukaryotic xMALPs using lipidomics and in-gel analysis. Our results show that the xMALPs content varies with the chemical properties of the used xMA and that some of these nanodiscs are less native than initially thought.<br>


2020 ◽  
Vol 118 (3) ◽  
pp. 361a-362a
Author(s):  
Benjamin D. Harding ◽  
Gunjan Dixit ◽  
Kevin M. Burridge ◽  
Gary A. Lorigan ◽  
Indra D. Sahu ◽  
...  

2019 ◽  
Vol 116 (3) ◽  
pp. 517a
Author(s):  
Benjamin D. Harding ◽  
Gunjan Dixit ◽  
Kevin M. Burridge ◽  
Indra D. Sahu ◽  
Carole Dabney-Smith ◽  
...  

2020 ◽  
Author(s):  
Marta Barniol-Xicota ◽  
Steven Verhelst

Membrane proteins are key in a large number of physiological and pathological processes. Their study often involves a prior detergent solubilization step, which strips away the membrane and can jeopardize membrane protein integrity. A recent alternative to detergents encompasses maleic acid based copolymers (xMAs), which disrupt the lipid bilayer and form lipid protein nanodiscs (xMALPs) soluble in aqueous buffer. Although xMALPs are often referred to as native nanodiscs, little is known about the resemblance of their lipid and protein content to the native bilayer. Here we have analyzed prokaryotic and eukaryotic xMALPs using lipidomics and in-gel analysis. Our results show that the xMALPs content varies with the chemical properties of the used xMA and that some of these nanodiscs are less native than initially thought.<br>


2021 ◽  
Vol 96-97 ◽  
pp. S83
Author(s):  
Masayuki Munekane ◽  
Wakana Yamaguchi ◽  
Kohei Sano ◽  
Toshihide Yamasaki ◽  
Masafumi Tanaka ◽  
...  

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