New penta-saccharide-bearing tripod amphiphiles for membrane protein structure studies

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

Standard

New penta-saccharide-bearing tripod amphiphiles for membrane protein structure studies. / Ehsan, Muhammad; Ghani, Lubna; Du, Yang; Hariharan, Parameswaran; Mortensen, Jonas S.; Ribeiro, Orquidea; Hu, Hongli; Skiniotis, Georgios; Loland, Claus J.; Guan, Lan; Kobilka, Brian K.; Byrne, Bernadette; Chae, Pil Seok.

In: Analyst, Vol. 142, No. 20, 10.2017, p. 3889-3898.

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

Harvard

Ehsan, M, Ghani, L, Du, Y, Hariharan, P, Mortensen, JS, Ribeiro, O, Hu, H, Skiniotis, G, Loland, CJ, Guan, L, Kobilka, BK, Byrne, B & Chae, PS 2017, 'New penta-saccharide-bearing tripod amphiphiles for membrane protein structure studies', Analyst, vol. 142, no. 20, pp. 3889-3898. https://doi.org/10.1039/c7an01168g

APA

Ehsan, M., Ghani, L., Du, Y., Hariharan, P., Mortensen, J. S., Ribeiro, O., Hu, H., Skiniotis, G., Loland, C. J., Guan, L., Kobilka, B. K., Byrne, B., & Chae, P. S. (2017). New penta-saccharide-bearing tripod amphiphiles for membrane protein structure studies. Analyst, 142(20), 3889-3898. https://doi.org/10.1039/c7an01168g

Vancouver

Ehsan M, Ghani L, Du Y, Hariharan P, Mortensen JS, Ribeiro O et al. New penta-saccharide-bearing tripod amphiphiles for membrane protein structure studies. Analyst. 2017 Oct;142(20):3889-3898. https://doi.org/10.1039/c7an01168g

Author

Ehsan, Muhammad ; Ghani, Lubna ; Du, Yang ; Hariharan, Parameswaran ; Mortensen, Jonas S. ; Ribeiro, Orquidea ; Hu, Hongli ; Skiniotis, Georgios ; Loland, Claus J. ; Guan, Lan ; Kobilka, Brian K. ; Byrne, Bernadette ; Chae, Pil Seok. / New penta-saccharide-bearing tripod amphiphiles for membrane protein structure studies. In: Analyst. 2017 ; Vol. 142, No. 20. pp. 3889-3898.

Bibtex

@article{ad61ed7b972c4ace86613ed8688d06da,
title = "New penta-saccharide-bearing tripod amphiphiles for membrane protein structure studies",
abstract = "Integral membrane proteins either alone or as complexes carry out a range of key cellular functions. Detergents are indispensable tools in the isolation of membrane proteins from biological membranes for downstream studies. Although a large number of techniques and tools, including a wide variety of detergents, are available, purification and structural characterization of many membrane proteins remain challenging. In the current study, a new class of tripod amphiphiles bearing two different penta-saccharide head groups, designated TPSs, were developed and evaluated for their ability to extract and stabilize a range of diverse membrane proteins. Variations in the structures of the detergent head and tail groups allowed us to prepare three sets of the novel agents with distinctive structures. Some TPSs (TPS-A8 and TPS-E7) were efficient at extracting two proteins in a functional state while others (TPS-E8 and TPS-E10L) conferred marked stability to all membrane proteins (and membrane protein complexes) tested here compared to a conventional detergent. Use of TPS-E10L led to clear visualization of a receptor-Gs complex using electron microscopy, indicating profound potential in membrane protein research.",
author = "Muhammad Ehsan and Lubna Ghani and Yang Du and Parameswaran Hariharan and Mortensen, {Jonas S.} and Orquidea Ribeiro and Hongli Hu and Georgios Skiniotis and Loland, {Claus J.} and Lan Guan and Kobilka, {Brian K.} and Bernadette Byrne and Chae, {Pil Seok}",
year = "2017",
month = oct,
doi = "10.1039/c7an01168g",
language = "English",
volume = "142",
pages = "3889--3898",
journal = "The Analyst",
issn = "0003-2654",
publisher = "Royal Society of Chemistry",
number = "20",

}

RIS

TY - JOUR

T1 - New penta-saccharide-bearing tripod amphiphiles for membrane protein structure studies

AU - Ehsan, Muhammad

AU - Ghani, Lubna

AU - Du, Yang

AU - Hariharan, Parameswaran

AU - Mortensen, Jonas S.

AU - Ribeiro, Orquidea

AU - Hu, Hongli

AU - Skiniotis, Georgios

AU - Loland, Claus J.

AU - Guan, Lan

AU - Kobilka, Brian K.

AU - Byrne, Bernadette

AU - Chae, Pil Seok

PY - 2017/10

Y1 - 2017/10

N2 - Integral membrane proteins either alone or as complexes carry out a range of key cellular functions. Detergents are indispensable tools in the isolation of membrane proteins from biological membranes for downstream studies. Although a large number of techniques and tools, including a wide variety of detergents, are available, purification and structural characterization of many membrane proteins remain challenging. In the current study, a new class of tripod amphiphiles bearing two different penta-saccharide head groups, designated TPSs, were developed and evaluated for their ability to extract and stabilize a range of diverse membrane proteins. Variations in the structures of the detergent head and tail groups allowed us to prepare three sets of the novel agents with distinctive structures. Some TPSs (TPS-A8 and TPS-E7) were efficient at extracting two proteins in a functional state while others (TPS-E8 and TPS-E10L) conferred marked stability to all membrane proteins (and membrane protein complexes) tested here compared to a conventional detergent. Use of TPS-E10L led to clear visualization of a receptor-Gs complex using electron microscopy, indicating profound potential in membrane protein research.

AB - Integral membrane proteins either alone or as complexes carry out a range of key cellular functions. Detergents are indispensable tools in the isolation of membrane proteins from biological membranes for downstream studies. Although a large number of techniques and tools, including a wide variety of detergents, are available, purification and structural characterization of many membrane proteins remain challenging. In the current study, a new class of tripod amphiphiles bearing two different penta-saccharide head groups, designated TPSs, were developed and evaluated for their ability to extract and stabilize a range of diverse membrane proteins. Variations in the structures of the detergent head and tail groups allowed us to prepare three sets of the novel agents with distinctive structures. Some TPSs (TPS-A8 and TPS-E7) were efficient at extracting two proteins in a functional state while others (TPS-E8 and TPS-E10L) conferred marked stability to all membrane proteins (and membrane protein complexes) tested here compared to a conventional detergent. Use of TPS-E10L led to clear visualization of a receptor-Gs complex using electron microscopy, indicating profound potential in membrane protein research.

U2 - 10.1039/c7an01168g

DO - 10.1039/c7an01168g

M3 - Journal article

C2 - 28913526

AN - SCOPUS:85031011601

VL - 142

SP - 3889

EP - 3898

JO - The Analyst

JF - The Analyst

SN - 0003-2654

IS - 20

ER -

ID: 188449369