Glycotripod Amphiphiles for Solubilization and Stabilization of a Membrane-Protein Superassembly: Importance of Branching in the Hydrophilic Portion
Three‐legged friends: Intrinsic membrane proteins must usually be extracted from the native membrane with the aid of synthetic amphiphiles and then stabilized before detailed structural and functional characterization is possible. We describe new amphiphiles with unusual architectures that were usef...
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Published in | Chembiochem : a European journal of chemical biology Vol. 9; no. 11; pp. 1706 - 1709 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
Weinheim
Wiley-VCH Verlag
21.07.2008
WILEY-VCH Verlag WILEY‐VCH Verlag |
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Abstract | Three‐legged friends: Intrinsic membrane proteins must usually be extracted from the native membrane with the aid of synthetic amphiphiles and then stabilized before detailed structural and functional characterization is possible. We describe new amphiphiles with unusual architectures that were useful for extraction and stabilization of protein superassemblies from bacterial membranes. Our results suggest that incorporation of branch points (as shown in figure) in both the hydrophilic and lipophilic portions can lead to favorable amphiphile behavior. |
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AbstractList | Intrinsic membrane proteins must usually be extracted from the native membrane with the aid of synthetic amphiphiles and then stabilized in a soluble form before detailed structural and functional characterization is possible. We describe new amphiphiles with unusual architectures that are useful for extraction and stabilization of photosynthetic protein superassemblies from bacterial membranes. Our results suggest that incorporating branch points in both the hydrophilic and lipophilic portions can lead to favorable amphiphile behavior. Three‐legged friends: Intrinsic membrane proteins must usually be extracted from the native membrane with the aid of synthetic amphiphiles and then stabilized before detailed structural and functional characterization is possible. We describe new amphiphiles with unusual architectures that were useful for extraction and stabilization of protein superassemblies from bacterial membranes. Our results suggest that incorporation of branch points (as shown in figure) in both the hydrophilic and lipophilic portions can lead to favorable amphiphile behavior. |
Author | Laible, Philip D. Wander, Marc J. Bowling, Aaron P. Gellman, Samuel H. Chae, Pil S. |
AuthorAffiliation | [b] Biosciences Division, Argonne National Laborotory 9700 South Cass Avenue, Argonne, IL 60439 [a] Department of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI 53706 (USA) |
AuthorAffiliation_xml | – name: [b] Biosciences Division, Argonne National Laborotory 9700 South Cass Avenue, Argonne, IL 60439 – name: [a] Department of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI 53706 (USA) |
Author_xml | – sequence: 1 fullname: Chae, Pil S – sequence: 2 fullname: Wander, Marc J – sequence: 3 fullname: Bowling, Aaron P – sequence: 4 fullname: Laible, Philip D – sequence: 5 fullname: Gellman, Samuel H |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/18576450$$D View this record in MEDLINE/PubMed |
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Snippet | Three‐legged friends: Intrinsic membrane proteins must usually be extracted from the native membrane with the aid of synthetic amphiphiles and then stabilized... Intrinsic membrane proteins must usually be extracted from the native membrane with the aid of synthetic amphiphiles and then stabilized in a soluble form... |
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SubjectTerms | amphiphiles Bacterial Proteins - chemistry Bacterial Proteins - metabolism Carbohydrates - chemical synthesis Carbohydrates - chemistry Carbohydrates - pharmacology Cell Membrane - chemistry Cell Membrane - metabolism detergent design membrane proteins Membrane Proteins - chemistry Membrane Proteins - metabolism Protein Binding - drug effects Rhodobacter capsulatus - chemistry Solubility - drug effects solubilization stabilization |
Title | Glycotripod Amphiphiles for Solubilization and Stabilization of a Membrane-Protein Superassembly: Importance of Branching in the Hydrophilic Portion |
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