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 inChembiochem : a European journal of chemical biology Vol. 9; no. 11; pp. 1706 - 1709
Main Authors Chae, Pil S, Wander, Marc J, Bowling, Aaron P, Laible, Philip D, Gellman, Samuel H
Format Journal Article
LanguageEnglish
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.
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)
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– name: [a] Department of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI 53706 (USA)
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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
URI https://api.istex.fr/ark:/67375/WNG-33FQ0PKN-Z/fulltext.pdf
https://onlinelibrary.wiley.com/doi/abs/10.1002%2Fcbic.200800169
https://www.ncbi.nlm.nih.gov/pubmed/18576450
https://search.proquest.com/docview/69316674
https://pubmed.ncbi.nlm.nih.gov/PMC3527902
Volume 9
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