| Membrane binding and structure of de novo designed alpha-helical cationic coiled-coil-forming peptides. | |
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MedLine Citation:
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PMID: 16680794 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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We introduce a de novo designed peptide model system that enables the systematic study of 1) the role of a membrane environment in coiled-coil peptide folding, 2) the impact of different domains of an alpha-helical coiled-coil heptad repeat on the interaction with membranes, and 3) the dynamics of coiled-coil peptide-membrane interactions depending on environmental conditions. Starting from an ideal alpha-helical coiled-coil peptide sequence, several positively charged analogues were designed that exhibit a high propensity toward negatively charged lipid membranes. Furthermore, these peptides differ in their ability to form a stable alpha-helical coiled-coil structure. The influence of a membrane environment on peptide folding is studied. All positively charged peptides show strong interactions with negatively charged membranes. This interaction induces an alpha-helical structure of the former random-coil peptides, as revealed by circular dichroism measurements. Furthermore, vesicle aggregation is induced by a coiled-coil interaction of vesicle-bound peptides. Dynamic light scattering experiments show that the strength of vesicle aggregation increases with the peptide's intrinsic ability to form a stable alpha-helical coiled coil. Thus, the peptide variant equipped with the strongest inter- and intra-helical coiled-coil interactions shows the strongest effect on vesicle aggregation. The secondary structure of this peptide in the membrane-bound state was studied as well as its effect on the phospholipids. Peptide conformation within the peptide-lipid aggregates was analyzed by (13)C cross-polarization magic-angle spinning NMR experiments. A uniformly (13)C- and (15)N-labeled Leu residue was introduced at position 12 of the peptide chain. The (13)C chemical shift and torsion angle measurements support the finding of an alpha-helical structure of the peptide in its membrane-bound state. Neither membrane leakage nor fusion was observed upon peptide binding, which is unusual for amphiphatic peptide structures. Our results lay the foundation for a systematic study of the influence of the alpha-helical coiled-coil folding motif in membrane-active events on a molecular level. |
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Authors:
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Toni Vagt; Olaf Zschörnig; Daniel Huster; Beate Koksch |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Chemphyschem : a European journal of chemical physics and physical chemistry Volume: 7 ISSN: 1439-4235 ISO Abbreviation: Chemphyschem Publication Date: 2006 Jun |
Date Detail:
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Created Date: 2006-06-06 Completed Date: 2007-07-12 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 100954211 Medline TA: Chemphyschem Country: Germany |
Other Details:
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Languages: eng Pagination: 1361-71 Citation Subset: IM |
Affiliation:
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Institute of Chemistry and Biochemistry-Organic Chemistry, Free University of Berlin, Takustrasse 3, 14195 Berlin, Germany. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Biophysics / methods Carbon Isotopes / chemistry Chemistry, Physical / methods Circular Dichroism Leucine / chemistry Lipids / chemistry Magnetic Resonance Spectroscopy Membranes, Artificial Molecular Conformation Molecular Sequence Data Peptides / chemistry* Phospholipids / chemistry Protein Folding Protein Structure, Secondary |
| Chemical | |
Reg. No./Substance:
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0/Carbon Isotopes; 0/Lipids; 0/Membranes, Artificial; 0/Peptides; 0/Phospholipids; 61-90-5/Leucine |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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