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Bolaamphiphile-class surfactants can stabilize and support the function of solubilized integral membrane proteins.
- Source :
-
Biochemistry [Biochemistry] 2009 Dec 15; Vol. 48 (49), pp. 11606-8. - Publication Year :
- 2009
-
Abstract
- Bolaamphiphile-class surfactants composed of two hydrophilic (maltoside) headgroups connected by long saturated alkyl chains were tested for their ability to stabilize a solubilized membrane protein, Escherichia coli diacylglycerol kinase (DAGK), and to sustain its native function. Members of this "Bis-MALT-C(18-28)" series were poor solubilizers of DAGK in the absence of conventional detergent. However, mixed micelles of the bolaamphiphiles with either dodecylphosphocholine or beta-n-decyl maltoside were more effective and enhanced DAGK's thermal stability relative to corresponding detergent-only conditions. Moreover, certain bolaamphiphiles were seen to be lipidlike by providing partial activation of DAGK's catalytic activity. Finally, addition of bolaamphiphiles to micellar NMR samples of DAGK did not result in a degradation of spectral quality, indicating their compatibility with high-resolution structural studies. To the best of our knowledge, this work represents the first documentation of the potential of bolaamphiphile-class surfactants for use in biochemical and biophysical studies of MPs.
- Subjects :
- Diacylglycerol Kinase physiology
Escherichia coli Proteins chemistry
Escherichia coli Proteins physiology
Membrane Proteins physiology
Micelles
Protein Stability
Solubility
Solutions
Thermodynamics
Diacylglycerol Kinase chemistry
Furans chemistry
Furans classification
Membrane Proteins chemistry
Pyridones chemistry
Pyridones classification
Surface-Active Agents chemistry
Surface-Active Agents classification
Subjects
Details
- Language :
- English
- ISSN :
- 1520-4995
- Volume :
- 48
- Issue :
- 49
- Database :
- MEDLINE
- Journal :
- Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 19908902
- Full Text :
- https://doi.org/10.1021/bi9018708