Document Detail


Protein-lipid interactions studied with designed transmembrane peptides: role of hydrophobic matching and interfacial anchoring.
MedLine Citation:
PMID:  14578043     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Biological membranes are characterized by a heterogeneous composition, which is not only manifested in the wide variety of their components, but also in aspects like the lateral organization, topology, and conformation of proteins and lipids. In bringing about the correct membrane structure, protein-lipid interactions can be expected to play a prominent role. The extent of hydrophobic matching between transmembrane protein segments and lipids potentially constitutes a versatile director of membrane organization, because a tendency to avoid hydrophobic mismatch could result in compensating adaptations such as tilt of the transmembrane segment or segregation into distinct domains. Also, interfacial interactions between lipid headgroups and the aromatic and charged residues that typically flank transmembrane domains may act as an organizing element. In this review, we discuss the numerous model studies that have systematically explored the influence of hydrophobic matching and interfacial anchoring on membrane structure. Designed peptides consisting of a polyleucine or polyleucine/alanine hydrophobic stretch, which is flanked on both sides by tryptophan or lysine residues, reflect the general layout of transmembrane protein segments. It is shown for phosphatidylcholine bilayers and for other model membranes that these peptides adapt a transmembrane topology without extensive peptide or lipid adaptations under conditions of hydrophobic matching, but that significant rearrangements can result from hydrophobic mismatch. Moreover, these effects depend on the nature of the flanking residues, implying a modulation of the mismatch response by interfacial interactions of the flanking residues. The implications of these model studies for the organization of biomembranes are discussed in the context of recent experiments with more complex systems.
Authors:
Maurits R R de Planque; J Antoinette Killian
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Review    
Journal Detail:
Title:  Molecular membrane biology     Volume:  20     ISSN:  0968-7688     ISO Abbreviation:  Mol. Membr. Biol.     Publication Date:    2003 Oct-Dec
Date Detail:
Created Date:  2003-10-27     Completed Date:  2004-07-08     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9430797     Medline TA:  Mol Membr Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  271-84     Citation Subset:  IM    
Affiliation:
Department of Biochemistry of Membranes, Center for Biomembranes and Lipid Enzymology, Institute of Biomembranes, Utrecht University, Utrecht, The Netherlands. m.r.r.deplanque@chem.uu.nl
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MeSH Terms
Descriptor/Qualifier:
Animals
Cell Membrane / metabolism
Humans
Hydrophobicity
Lipid Bilayers / chemistry,  metabolism
Membrane Lipids / chemistry*,  metabolism*
Membrane Proteins / chemistry*,  metabolism*
Protein Conformation
Chemical
Reg. No./Substance:
0/Lipid Bilayers; 0/Membrane Lipids; 0/Membrane Proteins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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