3,4-Bis(hydroxymethyl)hexane-1,6-diol-based Maltosides (HDMs) for Membrane-Protein Study: Importance of Detergent Rigidity-Flexibility Balance in Protein Stability

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

Standard

3,4-Bis(hydroxymethyl)hexane-1,6-diol-based Maltosides (HDMs) for Membrane-Protein Study : Importance of Detergent Rigidity-Flexibility Balance in Protein Stability. / Lee, Hyun Sung; Das, Manabendra; Mahler, Florian; Ahmed, Waqar; Wang, Haoqing; Mortensen, Jonas S.; Hariharan, Parameswaran; Ghani, Lubna; Byrne, Bernadette; Guan, Lan; Loland, Claus J.; Keller, Sandro; Chae, Pil Seok.

In: Chemistry - An Asian Journal, Vol. 17, No. 24, e202200941, 2022.

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

Harvard

Lee, HS, Das, M, Mahler, F, Ahmed, W, Wang, H, Mortensen, JS, Hariharan, P, Ghani, L, Byrne, B, Guan, L, Loland, CJ, Keller, S & Chae, PS 2022, '3,4-Bis(hydroxymethyl)hexane-1,6-diol-based Maltosides (HDMs) for Membrane-Protein Study: Importance of Detergent Rigidity-Flexibility Balance in Protein Stability', Chemistry - An Asian Journal, vol. 17, no. 24, e202200941. https://doi.org/10.1002/asia.202200941

APA

Lee, H. S., Das, M., Mahler, F., Ahmed, W., Wang, H., Mortensen, J. S., Hariharan, P., Ghani, L., Byrne, B., Guan, L., Loland, C. J., Keller, S., & Chae, P. S. (2022). 3,4-Bis(hydroxymethyl)hexane-1,6-diol-based Maltosides (HDMs) for Membrane-Protein Study: Importance of Detergent Rigidity-Flexibility Balance in Protein Stability. Chemistry - An Asian Journal, 17(24), [e202200941]. https://doi.org/10.1002/asia.202200941

Vancouver

Lee HS, Das M, Mahler F, Ahmed W, Wang H, Mortensen JS et al. 3,4-Bis(hydroxymethyl)hexane-1,6-diol-based Maltosides (HDMs) for Membrane-Protein Study: Importance of Detergent Rigidity-Flexibility Balance in Protein Stability. Chemistry - An Asian Journal. 2022;17(24). e202200941. https://doi.org/10.1002/asia.202200941

Author

Lee, Hyun Sung ; Das, Manabendra ; Mahler, Florian ; Ahmed, Waqar ; Wang, Haoqing ; Mortensen, Jonas S. ; Hariharan, Parameswaran ; Ghani, Lubna ; Byrne, Bernadette ; Guan, Lan ; Loland, Claus J. ; Keller, Sandro ; Chae, Pil Seok. / 3,4-Bis(hydroxymethyl)hexane-1,6-diol-based Maltosides (HDMs) for Membrane-Protein Study : Importance of Detergent Rigidity-Flexibility Balance in Protein Stability. In: Chemistry - An Asian Journal. 2022 ; Vol. 17, No. 24.

Bibtex

@article{57d58c09b81c4e07837276103ae6329a,
title = "3,4-Bis(hydroxymethyl)hexane-1,6-diol-based Maltosides (HDMs) for Membrane-Protein Study: Importance of Detergent Rigidity-Flexibility Balance in Protein Stability",
abstract = "Detergents have been major contributors to membrane-protein structural study for decades. However, membrane proteins solubilized in conventional detergents tend to aggregate or denature over time. Stability of large eukaryotic membrane proteins with complex structures tends to be particularly poor, necessitating development of novel detergents with improved properties. Here, we prepared a novel class of detergents, designated 3,4-bis(hydroxymethyl)hexane-1,6-diol-based maltosides (HDMs). When tested on three membrane proteins, including two G-protein-coupled receptors (GPCRs), the new detergents displayed significantly better behaviors compared with DDM. Moreover, the HDMs were superior or comparable to LMNG, an amphiphile widely used for GPCR structural study. An optimal balance of detergent rigidity vs. flexibility of the HDMs is likely responsible for their favorable behaviors toward membrane-protein stability. Thus, the current study not only introduces the HDMs, with significant potential for membrane-protein structural study, but also suggests a useful guideline for designing novel detergents for membrane-protein research.",
keywords = "amphiphiles, membrane proteins, molecular design, HDM, molecular flexibility, BETA(2)-ADRENERGIC RECEPTOR, FACIAL AMPHIPHILES, CRYSTAL-STRUCTURE, GNG AMPHIPHILES, STABILIZATION, CRYSTALLIZATION, SOLUBILIZATION, SURFACTANTS, SYSTEMS, YIELDS",
author = "Lee, {Hyun Sung} and Manabendra Das and Florian Mahler and Waqar Ahmed and Haoqing Wang and Mortensen, {Jonas S.} and Parameswaran Hariharan and Lubna Ghani and Bernadette Byrne and Lan Guan and Loland, {Claus J.} and Sandro Keller and Chae, {Pil Seok}",
year = "2022",
doi = "10.1002/asia.202200941",
language = "English",
volume = "17",
journal = "Chemistry - An Asian Journal",
issn = "1861-4728",
publisher = "Wiley",
number = "24",

}

RIS

TY - JOUR

T1 - 3,4-Bis(hydroxymethyl)hexane-1,6-diol-based Maltosides (HDMs) for Membrane-Protein Study

T2 - Importance of Detergent Rigidity-Flexibility Balance in Protein Stability

AU - Lee, Hyun Sung

AU - Das, Manabendra

AU - Mahler, Florian

AU - Ahmed, Waqar

AU - Wang, Haoqing

AU - Mortensen, Jonas S.

AU - Hariharan, Parameswaran

AU - Ghani, Lubna

AU - Byrne, Bernadette

AU - Guan, Lan

AU - Loland, Claus J.

AU - Keller, Sandro

AU - Chae, Pil Seok

PY - 2022

Y1 - 2022

N2 - Detergents have been major contributors to membrane-protein structural study for decades. However, membrane proteins solubilized in conventional detergents tend to aggregate or denature over time. Stability of large eukaryotic membrane proteins with complex structures tends to be particularly poor, necessitating development of novel detergents with improved properties. Here, we prepared a novel class of detergents, designated 3,4-bis(hydroxymethyl)hexane-1,6-diol-based maltosides (HDMs). When tested on three membrane proteins, including two G-protein-coupled receptors (GPCRs), the new detergents displayed significantly better behaviors compared with DDM. Moreover, the HDMs were superior or comparable to LMNG, an amphiphile widely used for GPCR structural study. An optimal balance of detergent rigidity vs. flexibility of the HDMs is likely responsible for their favorable behaviors toward membrane-protein stability. Thus, the current study not only introduces the HDMs, with significant potential for membrane-protein structural study, but also suggests a useful guideline for designing novel detergents for membrane-protein research.

AB - Detergents have been major contributors to membrane-protein structural study for decades. However, membrane proteins solubilized in conventional detergents tend to aggregate or denature over time. Stability of large eukaryotic membrane proteins with complex structures tends to be particularly poor, necessitating development of novel detergents with improved properties. Here, we prepared a novel class of detergents, designated 3,4-bis(hydroxymethyl)hexane-1,6-diol-based maltosides (HDMs). When tested on three membrane proteins, including two G-protein-coupled receptors (GPCRs), the new detergents displayed significantly better behaviors compared with DDM. Moreover, the HDMs were superior or comparable to LMNG, an amphiphile widely used for GPCR structural study. An optimal balance of detergent rigidity vs. flexibility of the HDMs is likely responsible for their favorable behaviors toward membrane-protein stability. Thus, the current study not only introduces the HDMs, with significant potential for membrane-protein structural study, but also suggests a useful guideline for designing novel detergents for membrane-protein research.

KW - amphiphiles

KW - membrane proteins

KW - molecular design

KW - HDM

KW - molecular flexibility

KW - BETA(2)-ADRENERGIC RECEPTOR

KW - FACIAL AMPHIPHILES

KW - CRYSTAL-STRUCTURE

KW - GNG AMPHIPHILES

KW - STABILIZATION

KW - CRYSTALLIZATION

KW - SOLUBILIZATION

KW - SURFACTANTS

KW - SYSTEMS

KW - YIELDS

U2 - 10.1002/asia.202200941

DO - 10.1002/asia.202200941

M3 - Journal article

C2 - 36253323

VL - 17

JO - Chemistry - An Asian Journal

JF - Chemistry - An Asian Journal

SN - 1861-4728

IS - 24

M1 - e202200941

ER -

ID: 326085221