A Minimal Hydrophobicity Is Needed To Employ Amphiphilic p(HPMA)-co-p(LMA) Random Copolymers in Membrane Research
- Publication type:
- Journal article
- Metadata:
-
- Autoren
- Michael Stangl
- Mirjam Hemmelmann
- Mareli Allmeroth
- Rudolf Zentel
- Dirk Schneider
- DOI
- 10.1021/bi401611f
- eISSN
- 1520-4995
- ISSN
- 0006-2960
- Ausgabe der Veröffentlichung
- 9
- Zeitschrift
- Biochemistry
- Sprache
- en
- Online publication date
- 2014
- Paginierung
- 1410 - 1419
- Datum der Veröffentlichung
- 2014
- Status
- Published
- Herausgeber
- American Chemical Society (ACS)
- Herausgeber URL
- http://dx.doi.org/10.1021/bi401611f
- Datum der Datenerfassung
- 2023
- Titel
- A Minimal Hydrophobicity Is Needed To Employ Amphiphilic p(HPMA)-co-p(LMA) Random Copolymers in Membrane Research
- Ausgabe der Zeitschrift
- 53
Data source: Crossref
- Other metadata sources:
-
- Abstract
- Because a polymer environment might be milder than a detergent micelle, amphiphilic polymers have attracted attention as alternatives to detergents in membrane biochemistry. The polymer poly[N-(2-hydroxypropyl)-methacrylamid] [p(HPMA)] has recently been modified with hydrophobic lauryl methacrylate (LMA) moieties, resulting in the synthesis of amphiphilic p(HPMA)-co-p(LMA) polymers. p(HPMA)-co-p(LMA) polymers with a LMA content of 5 or 15% have unstable hydrophobic cores. This, on one hand, promotes interactions of the hydrophobic LMA moieties with membranes, resulting in membrane rupture, but at the same time prevents formation of a hydrophobic, membrane mimetic environment that is sufficiently stable for the incorporation of transmembrane proteins. On the other hand, the p(HPMA)-co-p(LMA) polymer with a LMA content of 25% forms a stable hydrophobic core structure, which prevents hydrophobic interactions with membrane lipids but allows stable incorporation of membrane proteins. On the basis of our data, it becomes obvious that amphiphilic polymers have to have threshold hydrophobicities should an application in membrane protein research be anticipated.
- Addresses
- Institut für Pharmazie und Biochemie, Johannes Gutenberg-Universität Mainz , Johann-Joachim-Becher-Weg 30, 55128 Mainz, Germany.
- Autoren
- Michael Stangl
- Mirjam Hemmelmann
- Mareli Allmeroth
- Rudolf Zentel
- Dirk Schneider
- DOI
- 10.1021/bi401611f
- eISSN
- 1520-4995
- Externe Identifier
- PubMed Identifier: 24533898
- Open access
- false
- ISSN
- 0006-2960
- Ausgabe der Veröffentlichung
- 9
- Zeitschrift
- Biochemistry
- Schlüsselwörter
- Methacrylates
- Polymers
- Hydrophobic and Hydrophilic Interactions
- Sprache
- eng
- Medium
- Print-Electronic
- Online publication date
- 2014
- Paginierung
- 1410 - 1419
- Datum der Veröffentlichung
- 2014
- Status
- Published
- Datum der Datenerfassung
- 2014
- Titel
- A minimal hydrophobicity is needed to employ amphiphilic p(HPMA)-co-p(LMA) random copolymers in membrane research.
- Sub types
- Research Support, Non-U.S. Gov't
- Journal Article
- Ausgabe der Zeitschrift
- 53
Data source: Europe PubMed Central
- Abstract
- Because a polymer environment might be milder than a detergent micelle, amphiphilic polymers have attracted attention as alternatives to detergents in membrane biochemistry. The polymer poly[N-(2-hydroxypropyl)-methacrylamid] [p(HPMA)] has recently been modified with hydrophobic lauryl methacrylate (LMA) moieties, resulting in the synthesis of amphiphilic p(HPMA)-co-p(LMA) polymers. p(HPMA)-co-p(LMA) polymers with a LMA content of 5 or 15% have unstable hydrophobic cores. This, on one hand, promotes interactions of the hydrophobic LMA moieties with membranes, resulting in membrane rupture, but at the same time prevents formation of a hydrophobic, membrane mimetic environment that is sufficiently stable for the incorporation of transmembrane proteins. On the other hand, the p(HPMA)-co-p(LMA) polymer with a LMA content of 25% forms a stable hydrophobic core structure, which prevents hydrophobic interactions with membrane lipids but allows stable incorporation of membrane proteins. On the basis of our data, it becomes obvious that amphiphilic polymers have to have threshold hydrophobicities should an application in membrane protein research be anticipated.
- Autoren
- Michael Stangl
- Mirjam Hemmelmann
- Mareli Allmeroth
- Rudolf Zentel
- Dirk Schneider
- Autoren-URL
- https://www.ncbi.nlm.nih.gov/pubmed/24533898
- DOI
- 10.1021/bi401611f
- eISSN
- 1520-4995
- Ausgabe der Veröffentlichung
- 9
- Zeitschrift
- Biochemistry
- Schlüsselwörter
- Hydrophobic and Hydrophilic Interactions
- Methacrylates
- Polymers
- Sprache
- eng
- Country
- United States
- Paginierung
- 1410 - 1419
- Datum der Veröffentlichung
- 2014
- Status
- Published
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2014
- Titel
- A minimal hydrophobicity is needed to employ amphiphilic p(HPMA)-co-p(LMA) random copolymers in membrane research.
- Sub types
- Journal Article
- Research Support, Non-U.S. Gov't
- Ausgabe der Zeitschrift
- 53
Data source: PubMed
- Beziehungen:
- Property of