Evidence map›Paper›PMID 27743406›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2016

Mesitylene-Cored Glucoside Amphiphiles (MGAs) for Membrane Protein Studies: Importance of Alkyl Chain Density in Detergent Efficacy.

Kyung Ho Cho, Orquidea Ribeiro, Yang Du, Elena Tikhonova, Jonas S Mortensen, Kelsey Markham, Parameswaran Hariharan, Claus J Loland, Lan Guan, Brian K Kobilka and 2 more

Abstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

10 citing papers in PubMed.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors.

Kyung Ho ChoDepartment of Bionanotechnology, Hanyang University, Ansan, 15588, Korea.ORCID http://orcid.org/0000-0001-6038-0816
Orquidea RibeiroDepartment of Life Sciences, Imperial College London, London, SW7 2AZ, UK.ORCID http://orcid.org/0000-0003-0746-6666
Yang DuMolecular and Cellular Physiology, Stanford, CA, 94305, USA.ORCID http://orcid.org/0000-0001-5115-0736
Elena TikhonovaDepartment of Cell Physiology and Molecular Biophysics, Center for Membrane Protein Research, School of Medicine, Texas Tech University Health Sciences Center, Lubbock, TX, 79430, USA.ORCID http://orcid.org/0000-0002-7892-9173
Jonas S MortensenDepartment of Neuroscience and Pharmacology, University of Copenhagen, 2200, Copenhagen, Denmark.ORCID http://orcid.org/0000-0002-6743-276X
Kelsey MarkhamDepartment of Cell Physiology and Molecular Biophysics, Center for Membrane Protein Research, School of Medicine, Texas Tech University Health Sciences Center, Lubbock, TX, 79430, USA.
Parameswaran HariharanDepartment of Cell Physiology and Molecular Biophysics, Center for Membrane Protein Research, School of Medicine, Texas Tech University Health Sciences Center, Lubbock, TX, 79430, USA.ORCID http://orcid.org/0000-0002-6020-1547
Claus J LolandDepartment of Neuroscience and Pharmacology, University of Copenhagen, 2200, Copenhagen, Denmark.ORCID http://orcid.org/0000-0002-1773-1446
Lan GuanDepartment of Cell Physiology and Molecular Biophysics, Center for Membrane Protein Research, School of Medicine, Texas Tech University Health Sciences Center, Lubbock, TX, 79430, USA.ORCID http://orcid.org/0000-0002-2274-361X
Brian K KobilkaMolecular and Cellular Physiology, Stanford, CA, 94305, USA.ORCID http://orcid.org/0000-0001-5958-3990
Bernadette ByrneDepartment of Life Sciences, Imperial College London, London, SW7 2AZ, UK.ORCID http://orcid.org/0000-0001-9598-9832
Pil Seok ChaeDepartment of Bionanotechnology, Hanyang University, Ansan, 15588, Korea.ORCID http://orcid.org/0000-0003-1799-3304

Funding

THE MECHANISM OF BETA2 ADRENOCEPTOR ACTIVATIONR01NS028471 · NINDS · STANFORD UNIVERSITY · PI KOBILKA, BRIAN K · 1990 to 2021
$6.7M
Novel capture reagents for membrane protein structure determinationR01GM095538 · NIGMS · TEXAS TECH UNIVERSITY HEALTH SCIS CENTER · PI GUAN, LAN · 2010 to 2013
$1.2M
NIGMS NIH HHS R01 GM095538NINDS NIH HHS R01 NS028471
6 · The paper itself

Abstract

Detergents serve as useful tools for membrane protein structural and functional studies. Their amphipathic nature allows detergents to associate with the hydrophobic regions of membrane proteins whilst maintaining the proteins in aqueous solution. However, widely used conventional detergents are limited in their ability to maintain the structural integrity of membrane proteins and thus there are major efforts underway to develop novel agents with improved properties. We prepared mesitylene-cored glucoside amphiphiles (MGAs) with three alkyl chains and compared these agents with previously developed xylene-linked maltoside agents (XMAs) with two alkyl chains and a conventional detergent (DDM). When these agents were evaluated for four membrane proteins including a G protein-coupled receptor (GPCR), some agents such as MGA-C13 and MGA-C14 resulted in markedly enhanced stability of membrane proteins compared to both DDM and the XMAs. This favourable behaviour is due likely to the increased hydrophobic density provided by the extra alkyl chain. Thus, this study not only describes new glucoside agents with potential for membrane protein research, but also introduces a new detergent design principle for future development.

Indexed as

Benzene DerivativesDetergentsGlucosidesHydrophobic and Hydrophilic InteractionsMembrane ProteinsXylenesBenzene DerivativesDetergentsGlucosidesMembrane ProteinsmesityleneXylenesamphiphile designdetergentsmembrane proteinsprotein solubilisationprotein stabilization

Identifiers

PMID27743406
PMCPMC5500206

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.