Sequence-specific dimerization of a transmembrane helix in amphipol A8-35

Publication type:
Journal article
Metadata:
Autoren
  • Michael Stangl
  • Sebastian Unger
  • Sandro Keller
  • Dirk Schneider
Sammlungen
  • metadata
ISSN
1932-6203
Ausgabe der Veröffentlichung
10
Zeitschrift
PLoS one
Schlüsselwörter
  • 500 Naturwissenschaften
  • 500 Natural sciences and mathematics
Sprache
eng
Paginierung
e110970
Datum der Veröffentlichung
2014
Herausgeber
PLoS
Herausgeber URL
http://dx.doi.org/10.1371/journal.pone.0110970
Datum der Datenerfassung
2020
Datum, an dem der Datensatz öffentlich gemacht wurde
2020
Zugang
Public
Titel
Sequence-specific dimerization of a transmembrane helix in amphipol A8-35
Ausgabe der Zeitschrift
9

Data source: METADATA.UB

Other metadata sources:
Autoren
  • Michael Stangl
  • Sebastian Unger
  • Sandro Keller
  • Dirk Schneider
DOI
10.1371/journal.pone.0110970
Editoren
  • Dariush Hinderberger
eISSN
1932-6203
Ausgabe der Veröffentlichung
10
Zeitschrift
PLoS ONE
Sprache
en
Online publication date
2014
Paginierung
e110970 - e110970
Status
Published online
Herausgeber
Public Library of Science (PLoS)
Herausgeber URL
http://dx.doi.org/10.1371/journal.pone.0110970
Datum der Datenerfassung
2022
Titel
Sequence-Specific Dimerization of a Transmembrane Helix in Amphipol A8-35
Ausgabe der Zeitschrift
9

Data source: Crossref

Abstract
As traditional detergents might destabilize or even denature membrane proteins, amphiphilic polymers have moved into the focus of membrane-protein research in recent years. Thus far, Amphipols are the best studied amphiphilic copolymers, having a hydrophilic backbone with short hydrophobic chains. However, since stabilizing as well as destabilizing effects of the Amphipol belt on the structure of membrane proteins have been described, we systematically analyze the impact of the most commonly used Amphipol A8-35 on the structure and stability of a well-defined transmembrane protein model, the glycophorin A transmembrane helix dimer. Amphipols are not able to directly extract proteins from their native membranes, and detergents are typically replaced by Amphipols only after protein extraction from membranes. As Amphipols form mixed micelles with detergents, a better understanding of Amphipol-detergent interactions is required. Therefore, we analyze the interaction of A8-35 with the anionic detergent sodium dodecyl sulfate and describe the impact of the mixed-micelle-like system on the stability of a transmembrane helix dimer. As A8-35 may highly stabilize and thereby rigidify a transmembrane protein structure, modest destabilization by controlled addition of detergents and formation of mixed micellar systems might be helpful to preserve the function of a membrane protein in Amphipol environments.
Addresses
  • Department of Pharmacy and Biochemistry, Johannes-Gutenberg-University, Mainz, Germany.
Autoren
  • Michael Stangl
  • Sebastian Unger
  • Sandro Keller
  • Dirk Schneider
DOI
10.1371/journal.pone.0110970
eISSN
1932-6203
Externe Identifier
  • PubMed Identifier: 25347769
  • PubMed Central ID: PMC4210147
Open access
true
ISSN
1932-6203
Ausgabe der Veröffentlichung
10
Zeitschrift
PloS one
Schlüsselwörter
  • Humans
  • Propylamines
  • Polymers
  • Peptide Fragments
  • Membrane Proteins
  • Detergents
  • Protein Structure, Secondary
  • Kinetics
  • Micelles
  • Protein Interaction Domains and Motifs
  • Protein Multimerization
  • Hydrophobic and Hydrophilic Interactions
  • Glycophorins
Sprache
eng
Medium
Electronic-eCollection
Online publication date
2014
Open access status
Open Access
Paginierung
e110970
Datum der Veröffentlichung
2014
Status
Published
Publisher licence
CC BY
Datum der Datenerfassung
2014
Titel
Sequence-specific dimerization of a transmembrane helix in amphipol A8-35.
Sub types
  • research-article
  • Journal Article
Ausgabe der Zeitschrift
9

Files

https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0110970&type=printable https://europepmc.org/articles/PMC4210147?pdf=render

Data source: Europe PubMed Central

Abstract
As traditional detergents might destabilize or even denature membrane proteins, amphiphilic polymers have moved into the focus of membrane-protein research in recent years. Thus far, Amphipols are the best studied amphiphilic copolymers, having a hydrophilic backbone with short hydrophobic chains. However, since stabilizing as well as destabilizing effects of the Amphipol belt on the structure of membrane proteins have been described, we systematically analyze the impact of the most commonly used Amphipol A8-35 on the structure and stability of a well-defined transmembrane protein model, the glycophorin A transmembrane helix dimer. Amphipols are not able to directly extract proteins from their native membranes, and detergents are typically replaced by Amphipols only after protein extraction from membranes. As Amphipols form mixed micelles with detergents, a better understanding of Amphipol-detergent interactions is required. Therefore, we analyze the interaction of A8-35 with the anionic detergent sodium dodecyl sulfate and describe the impact of the mixed-micelle-like system on the stability of a transmembrane helix dimer. As A8-35 may highly stabilize and thereby rigidify a transmembrane protein structure, modest destabilization by controlled addition of detergents and formation of mixed micellar systems might be helpful to preserve the function of a membrane protein in Amphipol environments.
Date of acceptance
2014
Autoren
  • Michael Stangl
  • Sebastian Unger
  • Sandro Keller
  • Dirk Schneider
Autoren-URL
https://www.ncbi.nlm.nih.gov/pubmed/25347769
DOI
10.1371/journal.pone.0110970
eISSN
1932-6203
Externe Identifier
  • PubMed Central ID: PMC4210147
Ausgabe der Veröffentlichung
10
Zeitschrift
PLoS One
Schlüsselwörter
  • Detergents
  • Glycophorins
  • Humans
  • Hydrophobic and Hydrophilic Interactions
  • Kinetics
  • Membrane Proteins
  • Micelles
  • Peptide Fragments
  • Polymers
  • Propylamines
  • Protein Interaction Domains and Motifs
  • Protein Multimerization
  • Protein Structure, Secondary
Sprache
eng
Country
United States
Paginierung
e110970
PII
PONE-D-14-28770
Datum der Veröffentlichung
2014
Status
Published online
Datum, an dem der Datensatz öffentlich gemacht wurde
2015
Titel
Sequence-specific dimerization of a transmembrane helix in amphipol A8-35.
Sub types
  • Journal Article
Ausgabe der Zeitschrift
9

Data source: PubMed

Author's licence
CC-BY
Autoren
  • Michael Stangl
  • Sebastian Unger
  • Sandro Keller
  • Dirk Schneider
Hosting institution
Universitätsbibliothek Mainz
Sammlungen
  • DFG-OA-Publizieren (2012 - 2017)
Resource version
Published version
DOI
10.1371/journal.pone.0110970
Funding acknowledgements
  • DFG, Open Access-Publizieren Universität Mainz / Universitätsmedizin
File(s) embargoed
false
Open access
true
ISSN
1932-6203
Ausgabe der Veröffentlichung
10
Zeitschrift
PLoS one
Schlüsselwörter
  • 500 Naturwissenschaften
  • 500 Natural sciences and mathematics
Sprache
eng
Open access status
Open Access
Paginierung
e110970
Datum der Veröffentlichung
2014
Public URL
https://openscience.ub.uni-mainz.de/handle/20.500.12030/7860
Herausgeber
PLoS
Herausgeber URL
http://dx.doi.org/10.1371/journal.pone.0110970
Datum der Datenerfassung
2022
Datum, an dem der Datensatz öffentlich gemacht wurde
2022
Zugang
Public
Titel
Sequence-specific dimerization of a transmembrane helix in amphipol A8-35
Ausgabe der Zeitschrift
9

Files

sequencespecific_dimerization-20220914005324699.pdf

Data source: OPENSCIENCE.UB

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