Vitamin E-based glycoside amphiphiles for membrane protein structural studies

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Vitamin E-based glycoside amphiphiles for membrane protein structural studies. / Ehsan, Muhammad; Du, Yang; Molist, Iago; Seven, Alpay B.; Hariharan, Parameswaran; Mortensen, Jonas S.; Ghani, Lubna; Loland, Claus J.; Skiniotis, Georgios; Guan, Lan; Byrne, Bernadette; Kobilka, Brian K.; Chae, Pil Seok.

In: Organic and Biomolecular Chemistry, Vol. 16, No. 14, 2018, p. 2489-2498.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Ehsan, M, Du, Y, Molist, I, Seven, AB, Hariharan, P, Mortensen, JS, Ghani, L, Loland, CJ, Skiniotis, G, Guan, L, Byrne, B, Kobilka, BK & Chae, PS 2018, 'Vitamin E-based glycoside amphiphiles for membrane protein structural studies', Organic and Biomolecular Chemistry, vol. 16, no. 14, pp. 2489-2498. https://doi.org/10.1039/c8ob00270c

APA

Ehsan, M., Du, Y., Molist, I., Seven, A. B., Hariharan, P., Mortensen, J. S., Ghani, L., Loland, C. J., Skiniotis, G., Guan, L., Byrne, B., Kobilka, B. K., & Chae, P. S. (2018). Vitamin E-based glycoside amphiphiles for membrane protein structural studies. Organic and Biomolecular Chemistry, 16(14), 2489-2498. https://doi.org/10.1039/c8ob00270c

Vancouver

Ehsan M, Du Y, Molist I, Seven AB, Hariharan P, Mortensen JS et al. Vitamin E-based glycoside amphiphiles for membrane protein structural studies. Organic and Biomolecular Chemistry. 2018;16(14):2489-2498. https://doi.org/10.1039/c8ob00270c

Author

Ehsan, Muhammad ; Du, Yang ; Molist, Iago ; Seven, Alpay B. ; Hariharan, Parameswaran ; Mortensen, Jonas S. ; Ghani, Lubna ; Loland, Claus J. ; Skiniotis, Georgios ; Guan, Lan ; Byrne, Bernadette ; Kobilka, Brian K. ; Chae, Pil Seok. / Vitamin E-based glycoside amphiphiles for membrane protein structural studies. In: Organic and Biomolecular Chemistry. 2018 ; Vol. 16, No. 14. pp. 2489-2498.

Bibtex

@article{3cc43bc992424cbe91ea36609fadbfcc,
title = "Vitamin E-based glycoside amphiphiles for membrane protein structural studies",
abstract = "Membrane proteins play critical roles in a variety of cellular processes. For a detailed molecular level understanding of their biological functions and roles in disease, it is necessary to extract them from the native membranes. While the amphipathic nature of these bio-macromolecules presents technical challenges, amphiphilic assistants such as detergents serve as useful tools for membrane protein structural and functional studies. Conventional detergents are limited in their ability to maintain the structural integrity of membrane proteins and thus it is essential to develop novel agents with enhanced properties. Here, we designed and characterized a novel class of amphiphiles with vitamin E (i.e., α-tocopherol) as the hydrophobic tail group and saccharide units as the hydrophilic head group. Designated vitamin E-based glycosides (VEGs), these agents were evaluated for their ability to solubilize and stabilize a set of membrane proteins. VEG representatives not only conferred markedly enhanced stability to a diverse range of membrane proteins compared to conventional detergents, but VEG-3 also showed notable efficacy toward stabilization and visualization of a membrane protein complex. In addition to hydrophile-lipophile balance (HLB) of detergent molecules, the chain length and molecular geometry of the detergent hydrophobic group seem key factors in determining detergent efficacy for membrane protein (complex) stability.",
author = "Muhammad Ehsan and Yang Du and Iago Molist and Seven, {Alpay B.} and Parameswaran Hariharan and Mortensen, {Jonas S.} and Lubna Ghani and Loland, {Claus J.} and Georgios Skiniotis and Lan Guan and Bernadette Byrne and Kobilka, {Brian K.} and Chae, {Pil Seok}",
year = "2018",
doi = "10.1039/c8ob00270c",
language = "English",
volume = "16",
pages = "2489--2498",
journal = "Organic & Biomolecular Chemistry",
issn = "1470-4358",
publisher = "Royal Society of Chemistry",
number = "14",

}

RIS

TY - JOUR

T1 - Vitamin E-based glycoside amphiphiles for membrane protein structural studies

AU - Ehsan, Muhammad

AU - Du, Yang

AU - Molist, Iago

AU - Seven, Alpay B.

AU - Hariharan, Parameswaran

AU - Mortensen, Jonas S.

AU - Ghani, Lubna

AU - Loland, Claus J.

AU - Skiniotis, Georgios

AU - Guan, Lan

AU - Byrne, Bernadette

AU - Kobilka, Brian K.

AU - Chae, Pil Seok

PY - 2018

Y1 - 2018

N2 - Membrane proteins play critical roles in a variety of cellular processes. For a detailed molecular level understanding of their biological functions and roles in disease, it is necessary to extract them from the native membranes. While the amphipathic nature of these bio-macromolecules presents technical challenges, amphiphilic assistants such as detergents serve as useful tools for membrane protein structural and functional studies. Conventional detergents are limited in their ability to maintain the structural integrity of membrane proteins and thus it is essential to develop novel agents with enhanced properties. Here, we designed and characterized a novel class of amphiphiles with vitamin E (i.e., α-tocopherol) as the hydrophobic tail group and saccharide units as the hydrophilic head group. Designated vitamin E-based glycosides (VEGs), these agents were evaluated for their ability to solubilize and stabilize a set of membrane proteins. VEG representatives not only conferred markedly enhanced stability to a diverse range of membrane proteins compared to conventional detergents, but VEG-3 also showed notable efficacy toward stabilization and visualization of a membrane protein complex. In addition to hydrophile-lipophile balance (HLB) of detergent molecules, the chain length and molecular geometry of the detergent hydrophobic group seem key factors in determining detergent efficacy for membrane protein (complex) stability.

AB - Membrane proteins play critical roles in a variety of cellular processes. For a detailed molecular level understanding of their biological functions and roles in disease, it is necessary to extract them from the native membranes. While the amphipathic nature of these bio-macromolecules presents technical challenges, amphiphilic assistants such as detergents serve as useful tools for membrane protein structural and functional studies. Conventional detergents are limited in their ability to maintain the structural integrity of membrane proteins and thus it is essential to develop novel agents with enhanced properties. Here, we designed and characterized a novel class of amphiphiles with vitamin E (i.e., α-tocopherol) as the hydrophobic tail group and saccharide units as the hydrophilic head group. Designated vitamin E-based glycosides (VEGs), these agents were evaluated for their ability to solubilize and stabilize a set of membrane proteins. VEG representatives not only conferred markedly enhanced stability to a diverse range of membrane proteins compared to conventional detergents, but VEG-3 also showed notable efficacy toward stabilization and visualization of a membrane protein complex. In addition to hydrophile-lipophile balance (HLB) of detergent molecules, the chain length and molecular geometry of the detergent hydrophobic group seem key factors in determining detergent efficacy for membrane protein (complex) stability.

U2 - 10.1039/c8ob00270c

DO - 10.1039/c8ob00270c

M3 - Journal article

AN - SCOPUS:85045001169

VL - 16

SP - 2489

EP - 2498

JO - Organic & Biomolecular Chemistry

JF - Organic & Biomolecular Chemistry

SN - 1470-4358

IS - 14

ER -

ID: 209805959