Study of hydrophobic interactions between acylated proteins and phospholipid bilayers using BIACORE
| Autor: | Jean-Claude Mani, Joël Chopineau, Magali Jullien, Marie-Odile Roy, Martine Pugnière |
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| Rok vydání: | 2001 |
| Předmět: |
biology
Chemistry RNase P Acylation Fatty Acids Lipid Bilayers Lysine Phospholipid Ribonuclease Pancreatic Surface Plasmon Resonance Bovine pancreatic ribonuclease Hydrophobic effect chemistry.chemical_compound Biochemistry Structural Biology biology.protein Animals Cattle lipids (amino acids peptides and proteins) Ribonuclease Surface plasmon resonance Lipid bilayer Molecular Biology Phospholipids Protein Binding |
| Zdroj: | Journal of Molecular Recognition. 14:72-78 |
| ISSN: | 1099-1352 0952-3499 |
| DOI: | 10.1002/1099-1352(200101/02)14:1<72::aid-jmr519>3.0.co;2-2 |
| Popis: | Intracellular proteins of eukaryotic cells are frequently covalently modified by the addition of long chain fatty acids. These modifications are thought to allow otherwise soluble proteins to associate with membranes by lipid-lipid based hydrophobic interactions. The purpose of this work was to quantify the effect of acyl chain length on hydrophobic interactions between acylated proteins and phospholipid monolayers. The binding of an artificially acylated model protein to electrically neutral phospholipids was studied by surface plasmon resonance, using BIACORE. Kinetic rates for the binding of bovine pancreatic ribonuclease A (RNase A), monoacylated on its N-terminal lysine with fatty acids of 10, 12, 14, 16 or 18 carbon atoms, to phospholipids on hydrophobic sensor chips, were measured. Unlike unmodified ribonuclease, acylated RNase A bound to the phospholipids, and the association level increased with the acyl chain length to reach a maximum for C16. Reproducible kinetics were obtained which did not fit a 1:1 Langmuir model but rather a two-step binding profile. |
| Databáze: | OpenAIRE |
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