A comparative study of branched and linear mannitol-based amphiphiles on membrane protein stability

Hazrat Hussain; Tyler Helton; Yang Du; Jonas S. Mortensen; Parameswaran Hariharan; Muhammad Ehsan; Bernadette Byrne; Claus J. Loland; Brian K. Kobilka; Lan Guan; Pil Seok Chae

doi:10.1039/c8an01408f

A comparative study of branched and linear mannitol-based amphiphiles on membrane protein stability

Hazrat Hussain, Tyler Helton, Yang Du, Jonas S. Mortensen, Parameswaran Hariharan, Muhammad Ehsan, Bernadette Byrne, Claus J. Loland, Brian K. Kobilka, Lan Guan, Pil Seok Chae^*

^*Corresponding author af dette arbejde

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.

Originalsprog	Engelsk
Tidsskrift	Analyst
Vol/bind	143
Udgave nummer	23
Sider (fra-til)	5702-5710
Antal sider	9
ISSN	0003-2654
DOI	https://doi.org/10.1039/c8an01408f
Status	Udgivet - 2018

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10.1039/c8an01408f

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6242751/Licens: Andet

Citationsformater

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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",

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publisher = "Royal Society of Chemistry",

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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

SN - 0003-2654

VL - 143

SP - 5702

EP - 5710

JO - Analyst

JF - Analyst

IS - 23

ER -

A comparative study of branched and linear mannitol-based amphiphiles on membrane protein stability

Abstract

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