Diastereomeric Cyclopentane-Based Maltosides (CPMs) as Tools for Membrane Protein Study

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

Standard

Diastereomeric Cyclopentane-Based Maltosides (CPMs) as Tools for Membrane Protein Study. / Das, Manabendra; Mahler, Florian; Hariharan, Parameswaran; Wang, Haoqing; Du, Yang; Mortensen, Jonas S.; Patallo, Eugenio Pérez; Ghani, Lubna; Glück, David; Lee, Ho Jin; Byrne, Bernadette; Loland, Claus J.; Guan, Lan; Kobilka, Brian K.; Keller, Sandro; Chae, Pil Seok.

In: Journal of the American Chemical Society, Vol. 142, No. 51, 2020, p. 21382–21392.

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

Harvard

Das, M, Mahler, F, Hariharan, P, Wang, H, Du, Y, Mortensen, JS, Patallo, EP, Ghani, L, Glück, D, Lee, HJ, Byrne, B, Loland, CJ, Guan, L, Kobilka, BK, Keller, S & Chae, PS 2020, 'Diastereomeric Cyclopentane-Based Maltosides (CPMs) as Tools for Membrane Protein Study', Journal of the American Chemical Society, vol. 142, no. 51, pp. 21382–21392. https://doi.org/10.1021/jacs.0c09629

APA

Das, M., Mahler, F., Hariharan, P., Wang, H., Du, Y., Mortensen, J. S., Patallo, E. P., Ghani, L., Glück, D., Lee, H. J., Byrne, B., Loland, C. J., Guan, L., Kobilka, B. K., Keller, S., & Chae, P. S. (2020). Diastereomeric Cyclopentane-Based Maltosides (CPMs) as Tools for Membrane Protein Study. Journal of the American Chemical Society, 142(51), 21382–21392. https://doi.org/10.1021/jacs.0c09629

Vancouver

Das M, Mahler F, Hariharan P, Wang H, Du Y, Mortensen JS et al. Diastereomeric Cyclopentane-Based Maltosides (CPMs) as Tools for Membrane Protein Study. Journal of the American Chemical Society. 2020;142(51):21382–21392. https://doi.org/10.1021/jacs.0c09629

Author

Das, Manabendra ; Mahler, Florian ; Hariharan, Parameswaran ; Wang, Haoqing ; Du, Yang ; Mortensen, Jonas S. ; Patallo, Eugenio Pérez ; Ghani, Lubna ; Glück, David ; Lee, Ho Jin ; Byrne, Bernadette ; Loland, Claus J. ; Guan, Lan ; Kobilka, Brian K. ; Keller, Sandro ; Chae, Pil Seok. / Diastereomeric Cyclopentane-Based Maltosides (CPMs) as Tools for Membrane Protein Study. In: Journal of the American Chemical Society. 2020 ; Vol. 142, No. 51. pp. 21382–21392.

Bibtex

@article{09696f372be04b508e99d93d0cb984b9,
title = "Diastereomeric Cyclopentane-Based Maltosides (CPMs) as Tools for Membrane Protein Study",
abstract = "Amphiphilic agents, called detergents, are invaluable tools for studying membrane proteins. However, membrane proteins encapsulated by conventional head-to-tail detergents tend to denature or aggregate, necessitating the development of structurally distinct molecules with improved efficacy. Here, a novel class of diastereomeric detergents with a cyclopentane core unit, designated cyclopentane-based maltosides (CPMs), were prepared and evaluated for their ability to solubilize and stabilize several model membrane proteins. A couple of CPMs displayed enhanced behavior compared with the benchmark conventional detergent, n-dodecyl-β-d-maltoside (DDM), for all the tested membrane proteins including two G-protein-coupled receptors (GPCRs). Furthermore, CPM-C12 was notable for its ability to confer enhanced membrane protein stability compared with the previously developed conformationally rigid NBMs [J. Am. Chem. Soc. 2017, 139, 3072] and LMNG. The effect of the individual CPMs on protein stability varied depending on both the detergent configuration (cis/trans) and alkyl chain length, allowing us draw conclusions on the detergent structure-property-efficacy relationship. Thus, this study not only provides novel detergent tools useful for membrane protein research but also reports on structural features of the detergents critical for detergent efficacy in stabilizing membrane proteins. ",
author = "Manabendra Das and Florian Mahler and Parameswaran Hariharan and Haoqing Wang and Yang Du and Mortensen, {Jonas S.} and Patallo, {Eugenio P{\'e}rez} and Lubna Ghani and David Gl{\"u}ck and Lee, {Ho Jin} and Bernadette Byrne and Loland, {Claus J.} and Lan Guan and Kobilka, {Brian K.} and Sandro Keller and Chae, {Pil Seok}",
year = "2020",
doi = "10.1021/jacs.0c09629",
language = "English",
volume = "142",
pages = "21382–21392",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "ACS Publications",
number = "51",

}

RIS

TY - JOUR

T1 - Diastereomeric Cyclopentane-Based Maltosides (CPMs) as Tools for Membrane Protein Study

AU - Das, Manabendra

AU - Mahler, Florian

AU - Hariharan, Parameswaran

AU - Wang, Haoqing

AU - Du, Yang

AU - Mortensen, Jonas S.

AU - Patallo, Eugenio Pérez

AU - Ghani, Lubna

AU - Glück, David

AU - Lee, Ho Jin

AU - Byrne, Bernadette

AU - Loland, Claus J.

AU - Guan, Lan

AU - Kobilka, Brian K.

AU - Keller, Sandro

AU - Chae, Pil Seok

PY - 2020

Y1 - 2020

N2 - Amphiphilic agents, called detergents, are invaluable tools for studying membrane proteins. However, membrane proteins encapsulated by conventional head-to-tail detergents tend to denature or aggregate, necessitating the development of structurally distinct molecules with improved efficacy. Here, a novel class of diastereomeric detergents with a cyclopentane core unit, designated cyclopentane-based maltosides (CPMs), were prepared and evaluated for their ability to solubilize and stabilize several model membrane proteins. A couple of CPMs displayed enhanced behavior compared with the benchmark conventional detergent, n-dodecyl-β-d-maltoside (DDM), for all the tested membrane proteins including two G-protein-coupled receptors (GPCRs). Furthermore, CPM-C12 was notable for its ability to confer enhanced membrane protein stability compared with the previously developed conformationally rigid NBMs [J. Am. Chem. Soc. 2017, 139, 3072] and LMNG. The effect of the individual CPMs on protein stability varied depending on both the detergent configuration (cis/trans) and alkyl chain length, allowing us draw conclusions on the detergent structure-property-efficacy relationship. Thus, this study not only provides novel detergent tools useful for membrane protein research but also reports on structural features of the detergents critical for detergent efficacy in stabilizing membrane proteins.

AB - Amphiphilic agents, called detergents, are invaluable tools for studying membrane proteins. However, membrane proteins encapsulated by conventional head-to-tail detergents tend to denature or aggregate, necessitating the development of structurally distinct molecules with improved efficacy. Here, a novel class of diastereomeric detergents with a cyclopentane core unit, designated cyclopentane-based maltosides (CPMs), were prepared and evaluated for their ability to solubilize and stabilize several model membrane proteins. A couple of CPMs displayed enhanced behavior compared with the benchmark conventional detergent, n-dodecyl-β-d-maltoside (DDM), for all the tested membrane proteins including two G-protein-coupled receptors (GPCRs). Furthermore, CPM-C12 was notable for its ability to confer enhanced membrane protein stability compared with the previously developed conformationally rigid NBMs [J. Am. Chem. Soc. 2017, 139, 3072] and LMNG. The effect of the individual CPMs on protein stability varied depending on both the detergent configuration (cis/trans) and alkyl chain length, allowing us draw conclusions on the detergent structure-property-efficacy relationship. Thus, this study not only provides novel detergent tools useful for membrane protein research but also reports on structural features of the detergents critical for detergent efficacy in stabilizing membrane proteins.

U2 - 10.1021/jacs.0c09629

DO - 10.1021/jacs.0c09629

M3 - Journal article

C2 - 33315387

AN - SCOPUS:85098875714

VL - 142

SP - 21382

EP - 21392

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

IS - 51

ER -

ID: 255727431