Solution conformation of the synthetic bovine proenkephalin-A209-237 by 1H NMR spectroscopy
| Autor: | Baudoin Dillmann, Yannick Goumon, Marie-Hélène Metz-Boutigue, Bruno Kieffer, Jean-François Lefèvre, Dominique Aunis |
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| Rok vydání: | 1998 |
| Předmět: |
Models
Molecular 1h nmr spectroscopy Magnetic Resonance Spectroscopy Stereochemistry Protein Conformation Molecular Sequence Data Static Electricity Peptide Biochemistry Residue (chemistry) Molecule Animals Proline Amino Acid Sequence Protein Precursors Molecular Biology chemistry.chemical_classification Cell Biology Enkephalins Nmr data Proenkephalin Solutions chemistry Cattle Protons Antibacterial activity |
| Zdroj: | The Journal of biological chemistry. 273(50) |
| ISSN: | 0021-9258 |
| Popis: | Proenkephalin-A has been described to generate enkephalins, opoid peptides, and several derived peptides, which display various biological effects, including antinociception and immunological enhancement. Recently, we have isolated from bovine chromaffin granules a new antibacterial peptide, named enkelytin, which corresponds to the bisphosphorylated form of PEAP209-237 (Goumon, Y., Strub, J. M., Moniatte, M., Nullans, G., Poteur, L., Hubert, P., Van Dorsselaer, A., Aunis, D., and Metz-Boutigue, M. H. (1996) Eur. J. Biochem. 235, 516-525). In this paper, the three-dimensional solution structure of synthetic PEAP209-237 was investigated by NMR. These studies indicate that this peptide, which is unstructured in water, folds into an alpha-helical structure in trifluoroethanol/water (1/1). NMR data revealed two possible three-dimensional models of PEAP209-237. In both models, the proline residue Pro-227 induces a 90 degrees hinge between two alpha-helical segments (Ser-215 to Ser-221 and Glu-228 to Arg-232) leading to an overall L-shaped structure for the molecule. The negative charge of PEAP209-237 and the low amphipathy of the two alpha-helical segments imply new mechanisms to explain the antibacterial activity of enkelytin. |
| Databáze: | OpenAIRE |
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