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 journalJournal articleResearchpeer-review

Harvard

Hussain, H, Helton, T, Du, Y, Mortensen, JS, Hariharan, P, Ehsan, M, Byrne, B, Loland, CJ, Kobilka, BK, Guan, L & Chae, PS 2018, 'A comparative study of branched and linear mannitol-based amphiphiles on membrane protein stability', Analyst, vol. 143, no. 23, pp. 5702-5710. https://doi.org/10.1039/c8an01408f

APA

Hussain, H., Helton, T., Du, Y., Mortensen, J. S., Hariharan, P., Ehsan, M., Byrne, B., Loland, C. J., Kobilka, B. K., Guan, L., & Chae, P. S. (2018). A comparative study of branched and linear mannitol-based amphiphiles on membrane protein stability. Analyst, 143(23), 5702-5710. https://doi.org/10.1039/c8an01408f

Vancouver

Hussain H, Helton T, Du Y, Mortensen JS, Hariharan P, Ehsan M et al. A comparative study of branched and linear mannitol-based amphiphiles on membrane protein stability. Analyst. 2018;143(23):5702-5710. https://doi.org/10.1039/c8an01408f

Author

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. / A comparative study of branched and linear mannitol-based amphiphiles on membrane protein stability. In: Analyst. 2018 ; Vol. 143, No. 23. pp. 5702-5710.

Bibtex

@article{bd05d2afe09642f297778894d5e4e675,
title = "A comparative study of branched and linear mannitol-based amphiphiles on membrane protein stability",
abstract = "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.",
author = "Hazrat Hussain and Tyler Helton and Yang Du and Mortensen, {Jonas S.} and Parameswaran Hariharan and Muhammad Ehsan and Bernadette Byrne and Loland, {Claus J.} and Kobilka, {Brian K.} and Lan Guan and Chae, {Pil Seok}",
year = "2018",
doi = "10.1039/c8an01408f",
language = "English",
volume = "143",
pages = "5702--5710",
journal = "The Analyst",
issn = "0003-2654",
publisher = "Royal Society of Chemistry",
number = "23",

}

RIS

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