Interaction of Horse Heart and Thermus thermophilus Type c Cytochromes with Phospholipid Vesicles and Hydrophobic Surfaces
| Autor: | Sophie Lecomte, Maïté Paternostre, Marie-Hélène Baron, Silke Oellerich, Sophie Bernad, Tewfik Soulimane, Sylvie Noinville |
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| Přispěvatelé: | Laboratoire de Dynamique Interactions et Réactivité (LADIR), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2004 |
| Předmět: |
Models
Molecular MESH: Animals Cytochrome c Group / chemistry* Equidae / metabolism Hydrophobic and Hydrophilic Interactions Liposomes / chemistry* Models Molecular* Phosphatidylglycerols / chemistry* Phospholipids / chemistry* Protein Structure Secondary Silanes / chemistry Spectroscopy Fourier Transform Infrared Thermus thermophilus / chemistry Cytochrome [SDV]Life Sciences [q-bio] Biophysics Analytical chemistry Cytochrome c Group 010402 general chemistry 01 natural sciences environment and public health Protein Structure Secondary Hydrophobic effect 03 medical and health sciences chemistry.chemical_compound Spectroscopy Fourier Transform Infrared Animals [CHIM]Chemical Sciences Protein secondary structure Phospholipids 030304 developmental biology Phosphatidylglycerol 0303 health sciences Liposome biology Cytochrome c Vesicle Thermus thermophilus Proteins Phosphatidylglycerols Equidae Silanes biology.organism_classification 0104 chemical sciences enzymes and coenzymes (carbohydrates) chemistry Liposomes embryonic structures biology.protein cardiovascular system Hydrophobic and Hydrophilic Interactions |
| Zdroj: | Biophysical Journal Biophysical Journal, Biophysical Society, 2004, 86 (6), pp.3863-3872. ⟨10.1529/biophysj.103.025114⟩ Biophysical Journal, 2004, 86 (6), pp.3863-3872. ⟨10.1529/biophysj.103.025114⟩ |
| ISSN: | 0006-3495 1542-0086 |
| DOI: | 10.1529/biophysj.103.025114⟩ |
| Popis: | International audience; The binding of horse heart cytochrome c (cyt-c) and Thermus thermophilus cytochrome c552 (cyt-c552) to dioleoyl phosphatidylglycerol (DOPG) vesicles was investigated using Fourier transform infrared (FTIR) spectroscopy and turbidity measurements. FTIR spectra revealed that the tertiary structures of both cytochromes became more open when bound to DOPG vesicles, but this was more pronounced for cyt-c. Their secondary structures were unchanged. Turbidity measurements showed important differences in their behavior bound to the negatively charged DOPG vesicles. Both cytochromes caused the liposomes to aggregate and flocculate, but the ways they did so differed. For cyt-c, more than a monolayer was adsorbed onto the liposome surface prior to aggregation due to charge neutralization, whereas cyt c552 caused aggregation at a protein/lipid ratio well below that required for charge neutralization. Therefore, although cyt-c may cause liposomes to aggregate by electrostatic interaction, cyt-c552 does not act in this way. FTIR-attenuated total reflection spectroscopy (FTIR-ATR) revealed that cyt-c lost much of its secondary structure when bound to the hydrophobic surface of octadecyltrichlorosilane, whereas cyt-c552 folds its domains into a {beta}-structure. This hydrophobic effect may be the key to the difference between the behaviors of the two cytochromes when bound to DOPG vesicles. |
| Databáze: | OpenAIRE |
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