Novel Xylene-Linked Maltoside Amphiphiles (XMAs) for Membrane Protein Stabilisation

Research output: Contribution to journal › Letter › Research › peer-review

Standard

Novel Xylene-Linked Maltoside Amphiphiles (XMAs) for Membrane Protein Stabilisation. / Cho, Kyung Ho; Du, Yang; Scull, Nicola J; Hariharan, Parameswaran; Gotfryd, Kamil; Loland, Claus J; Guan, Lan; Byrne, Bernadette; Kobilka, Brian K; Chae, Pil Seok.

In: Chemistry: A European Journal, Vol. 21, No. 28, 2015, p. 10008–10013 .

Research output: Contribution to journal › Letter › Research › peer-review

Harvard

Cho, KH, Du, Y, Scull, NJ, Hariharan, P, Gotfryd, K, Loland, CJ, Guan, L, Byrne, B, Kobilka, BK & Chae, PS 2015, 'Novel Xylene-Linked Maltoside Amphiphiles (XMAs) for Membrane Protein Stabilisation', Chemistry: A European Journal, vol. 21, no. 28, pp. 10008–10013 . https://doi.org/10.1002/chem.201501083

APA

Cho, K. H., Du, Y., Scull, N. J., Hariharan, P., Gotfryd, K., Loland, C. J., Guan, L., Byrne, B., Kobilka, B. K., & Chae, P. S. (2015). Novel Xylene-Linked Maltoside Amphiphiles (XMAs) for Membrane Protein Stabilisation. Chemistry: A European Journal, 21(28), 10008–10013 . https://doi.org/10.1002/chem.201501083

Vancouver

Cho KH, Du Y, Scull NJ, Hariharan P, Gotfryd K, Loland CJ et al. Novel Xylene-Linked Maltoside Amphiphiles (XMAs) for Membrane Protein Stabilisation. Chemistry: A European Journal. 2015;21(28):10008–10013 . https://doi.org/10.1002/chem.201501083

Author

Cho, Kyung Ho ; Du, Yang ; Scull, Nicola J ; Hariharan, Parameswaran ; Gotfryd, Kamil ; Loland, Claus J ; Guan, Lan ; Byrne, Bernadette ; Kobilka, Brian K ; Chae, Pil Seok. / Novel Xylene-Linked Maltoside Amphiphiles (XMAs) for Membrane Protein Stabilisation. In: Chemistry: A European Journal. 2015 ; Vol. 21, No. 28. pp. 10008–10013 .

Bibtex

@article{ae9ba5e357b44a1ab0d5b5032292b9f3,
title = "Novel Xylene-Linked Maltoside Amphiphiles (XMAs) for Membrane Protein Stabilisation",
abstract = "Membrane proteins are key functional players in biological systems. These biomacromolecules contain both hydrophilic and hydrophobic regions and thus amphipathic molecules are necessary to extract membrane proteins from their native lipid environments and stabilise them in aqueous solutions. Conventional detergents are commonly used for membrane protein manipulation, but membrane proteins surrounded by these agents often undergo denaturation and aggregation. In this study, a novel class of maltoside-bearing amphiphiles, with a xylene linker in the central region, designated xylene-linked maltoside amphiphiles (XMAs) was developed. When these novel agents were evaluated with a number of membrane proteins, it was found that XMA-4 and XMA-5 have particularly favourable efficacy with respect to membrane protein stabilisation, indicating that these agents hold significant potential for membrane protein structural study.",
author = "Cho, {Kyung Ho} and Yang Du and Scull, {Nicola J} and Parameswaran Hariharan and Kamil Gotfryd and Loland, {Claus J} and Lan Guan and Bernadette Byrne and Kobilka, {Brian K} and Chae, {Pil Seok}",
note = "{\textcopyright} 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.",
year = "2015",
doi = "10.1002/chem.201501083",
language = "English",
volume = "21",
pages = "10008–10013 ",
journal = "Chemistry: A European Journal",
issn = "0947-6539",
publisher = "Wiley - V C H Verlag GmbH & Co. KGaA",
number = "28",

}

RIS

TY - JOUR

T1 - Novel Xylene-Linked Maltoside Amphiphiles (XMAs) for Membrane Protein Stabilisation

AU - Cho, Kyung Ho

AU - Du, Yang

AU - Scull, Nicola J

AU - Hariharan, Parameswaran

AU - Gotfryd, Kamil

AU - Loland, Claus J

AU - Guan, Lan

AU - Byrne, Bernadette

AU - Kobilka, Brian K

AU - Chae, Pil Seok

N1 - © 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

PY - 2015

Y1 - 2015

N2 - Membrane proteins are key functional players in biological systems. These biomacromolecules contain both hydrophilic and hydrophobic regions and thus amphipathic molecules are necessary to extract membrane proteins from their native lipid environments and stabilise them in aqueous solutions. Conventional detergents are commonly used for membrane protein manipulation, but membrane proteins surrounded by these agents often undergo denaturation and aggregation. In this study, a novel class of maltoside-bearing amphiphiles, with a xylene linker in the central region, designated xylene-linked maltoside amphiphiles (XMAs) was developed. When these novel agents were evaluated with a number of membrane proteins, it was found that XMA-4 and XMA-5 have particularly favourable efficacy with respect to membrane protein stabilisation, indicating that these agents hold significant potential for membrane protein structural study.

AB - Membrane proteins are key functional players in biological systems. These biomacromolecules contain both hydrophilic and hydrophobic regions and thus amphipathic molecules are necessary to extract membrane proteins from their native lipid environments and stabilise them in aqueous solutions. Conventional detergents are commonly used for membrane protein manipulation, but membrane proteins surrounded by these agents often undergo denaturation and aggregation. In this study, a novel class of maltoside-bearing amphiphiles, with a xylene linker in the central region, designated xylene-linked maltoside amphiphiles (XMAs) was developed. When these novel agents were evaluated with a number of membrane proteins, it was found that XMA-4 and XMA-5 have particularly favourable efficacy with respect to membrane protein stabilisation, indicating that these agents hold significant potential for membrane protein structural study.

U2 - 10.1002/chem.201501083

DO - 10.1002/chem.201501083

M3 - Letter

C2 - 26013293

VL - 21

SP - 10008

EP - 10013

JO - Chemistry: A European Journal

JF - Chemistry: A European Journal

SN - 0947-6539

IS - 28

ER -

ID: 138492919