A comparative study of branched and linear mannitol-based amphiphiles on membrane protein stability
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A comparative study of branched and linear mannitol-based amphiphiles on membrane protein stability. / Hussain, Hazrat; Helton, Tyler; Du, Yang; Mortensen, Jonas S.; Hariharan, Parameswaran; Ehsan, Muhammad; Byrne, Bernadette; Loland, Claus J.; Kobilka, Brian K.; Guan, Lan; Chae, Pil Seok.
In: Analyst, Vol. 143, No. 23, 2018, p. 5702-5710.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - A comparative study of branched and linear mannitol-based amphiphiles on membrane protein stability
AU - Hussain, Hazrat
AU - Helton, Tyler
AU - Du, Yang
AU - Mortensen, Jonas S.
AU - Hariharan, Parameswaran
AU - Ehsan, Muhammad
AU - Byrne, Bernadette
AU - Loland, Claus J.
AU - Kobilka, Brian K.
AU - Guan, Lan
AU - Chae, Pil Seok
PY - 2018
Y1 - 2018
N2 - The study of membrane proteins is extremely challenging, mainly because of the incompatibility of the hydrophobic surfaces of membrane proteins with an aqueous medium. Detergents are essential agents used to maintain membrane protein stability in non-native environments. However, conventional detergents fail to stabilize the native structures of many membrane proteins. Development of new amphipathic agents with enhanced efficacy for membrane protein stabilization is necessary to address this important problem. We have designed and synthesized linear and branched mannitol-based amphiphiles (MNAs), and comparative studies showed that most of the branched MNAs had advantages over the linear agents in terms of membrane protein stability. In addition, a couple of the new MNAs displayed favorable behaviors compared to n-dodecyl-β-d-maltoside and the previously developed MNAs in maintaining the native protein structures, indicating potential utility of these new agents in membrane protein study.
AB - The study of membrane proteins is extremely challenging, mainly because of the incompatibility of the hydrophobic surfaces of membrane proteins with an aqueous medium. Detergents are essential agents used to maintain membrane protein stability in non-native environments. However, conventional detergents fail to stabilize the native structures of many membrane proteins. Development of new amphipathic agents with enhanced efficacy for membrane protein stabilization is necessary to address this important problem. We have designed and synthesized linear and branched mannitol-based amphiphiles (MNAs), and comparative studies showed that most of the branched MNAs had advantages over the linear agents in terms of membrane protein stability. In addition, a couple of the new MNAs displayed favorable behaviors compared to n-dodecyl-β-d-maltoside and the previously developed MNAs in maintaining the native protein structures, indicating potential utility of these new agents in membrane protein study.
U2 - 10.1039/c8an01408f
DO - 10.1039/c8an01408f
M3 - Journal article
C2 - 30334564
AN - SCOPUS:85056603773
VL - 143
SP - 5702
EP - 5710
JO - The Analyst
JF - The Analyst
SN - 0003-2654
IS - 23
ER -
ID: 209800381