Androctonin, a Novel Antimicrobial Peptide from Scorpion Androctonus Australis : Solution Structure and Molecular Dynamics Simulations in the Presence of a Lipid Monolayer
| Autor: | Denise Sy, Charles Hetru, Nicolas Mandard, Françoise Vovelle, Philippe Bulet, Jean-Marc Bonmatin, Corinne Maufrais |
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| Přispěvatelé: | Centre de biophysique moléculaire (CBM), Université d'Orléans (UO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC) |
| Jazyk: | angličtina |
| Rok vydání: | 1999 |
| Předmět: |
Models
Molecular Magnetic Resonance Spectroscopy Stereochemistry Androctonus australis [SDV]Life Sciences [q-bio] Molecular Sequence Data Peptide 010402 general chemistry Peptides Cyclic 01 natural sciences Protein Structure Secondary Scorpions Turn (biochemistry) Membrane Lipids 03 medical and health sciences Molecular dynamics Structural Biology Amphiphile Monolayer Animals Amino Acid Sequence Molecular Biology 030304 developmental biology chemistry.chemical_classification 0303 health sciences Sequence Homology Amino Acid biology Proteins General Medicine biology.organism_classification Anti-Bacterial Agents 0104 chemical sciences Amino acid DNA-Binding Proteins chemistry Insect Proteins Antimicrobial Cationic Peptides Cysteine |
| Zdroj: | Journal of Biomolecular Structure and Dynamics Journal of Biomolecular Structure and Dynamics, Taylor & Francis: STM, Behavioural Science and Public Health Titles, 1999, 17 (2), pp.367-380. ⟨10.1080/07391102.1999.10508368⟩ |
| ISSN: | 0739-1102 1538-0254 |
| DOI: | 10.1080/07391102.1999.10508368⟩ |
| Popis: | International audience; Androctonin is a highly cationic antimicrobial peptide from scorpion exhibiting a broad spectrum of activities against bacteria and fungi. It contains 25 amino acids including four cysteine residues forming two disulfide bridges. We report here on the determination of its solution structure by conventional two-dimensional (2D) 1H-NMR spectroscopy and molecular modelling using distance geometry and molecular dynamics methods. The structure of androctonin involves a well-defined highly twisted anti-parallel beta-sheet with strands connected by a more variable positively charged turn. A comparison with the structure of tachyplesin I (horseshoe crab) reveals that the amphiphilic character of the protein surface of this homologous peptide is not observed in androctonin. We have undertaken a 200-ps molecular dynamics simulation study on a system including one androctonin molecule and a monolayer of DMPG (1,2-dimyristoylphosphatidylglycerol) lipids. On the basis of this simulation, the first steps of the membrane permeabilization process are discussed. |
| Databáze: | OpenAIRE |
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