| Protein-lipid interactions studied with designed transmembrane peptides: role of hydrophobic matching and interfacial anchoring. | |
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MedLine Citation:
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PMID: 14578043 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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Maurits R R de Planque; J Antoinette Killian |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Review |
Journal Detail:
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Title: Molecular membrane biology Volume: 20 ISSN: 0968-7688 ISO Abbreviation: Mol. Membr. Biol. Publication Date: 2003 Oct-Dec |
Date Detail:
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Created Date: 2003-10-27 Completed Date: 2004-07-08 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 9430797 Medline TA: Mol Membr Biol Country: England |
Other Details:
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Languages: eng Pagination: 271-84 Citation Subset: IM |
Affiliation:
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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 |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Cell Membrane / metabolism Humans Hydrophobicity Lipid Bilayers / chemistry, metabolism Membrane Lipids / chemistry*, metabolism* Membrane Proteins / chemistry*, metabolism* Protein Conformation |
| Chemical | |
Reg. No./Substance:
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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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