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alpha-Helical transmembrane peptides: A "Divide and Conquer" approach to membrane proteins.
MedLine Citation:
PMID:  19682979     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
alpha-Helical membrane proteins fulfill many vital roles in all living cells and constitute the majority of drug targets. However, their relevance is in no way paralleled by our current understanding of their structures and functions. This is because membrane proteins present a number of experimental obstacles that are difficult to surmount by classical methods developed for water-soluble proteins. Moreover, membrane proteins are not only challenging on their very own but, when embedded in a biological membrane, also reside in an outstandingly complex milieu. These difficulties have fostered a "divide and conquer" approach, in which a membrane protein is dissected into shorter and easier-to-handle transmembrane (TM) peptides. Under suitable conditions, such peptides fold independently and retain many of the properties displayed in the context of the full-length parent protein. This contribution reviews some of the most notable insights into alpha-helical membrane proteins gleaned from experiments on protein-derived TM peptides. We recapitulate some peculiar properties of lipid bilayers that render them such a complex and unique environment and discuss generic features pertaining to hydrophobic peptides derived from alpha-helical membrane proteins. The main part of the review is devoted to a critical discussion of particularly interesting examples of TM peptides studied in membrane-mimetic systems of increasing complexity: isotropic solvents, detergent micelles, lipid bilayers, and biological membranes. The unifying theme is to explore to what extent TM peptides in combination with different membrane-mimetic systems can aid in advancing our knowledge and comprehension of alpha-helical membrane proteins as well as in developing new pharmacological tools.
Authors:
Natalie Bordag; Sandro Keller
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Chemistry and physics of lipids     Volume:  163     ISSN:  1873-2941     ISO Abbreviation:  Chem. Phys. Lipids     Publication Date:  2010 Jan 
Date Detail:
Created Date:  2009-12-16     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0067206     Medline TA:  Chem Phys Lipids     Country:  Ireland    
Other Details:
Languages:  eng     Pagination:  1-26     Citation Subset:  IM    
Affiliation:
Leibniz Institute of Molecular Pharmacology FMP, Robert-Rössle-Str. 10, 13125 Berlin, Germany.
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