Peptides corresponding to the N- and C-terminal parts of PEBP are well-structured in solution: new insights into their possible interaction with partners in vivo
| Autor: | H. Labbé, Françoise Vovelle, Denise Sy, G Coadou, Françoise Schoentgen, Béatrice Vallée |
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| Rok vydání: | 2008 |
| Předmět: |
chemistry.chemical_classification
0303 health sciences Circular dichroism Peptide Nuclear magnetic resonance spectroscopy Crystal structure Biology Biochemistry Fluorescence 03 medical and health sciences Phosphatidylethanolamine Binding Protein 0302 clinical medicine Endocrinology chemistry Monolayer Biophysics Peptide sequence 030217 neurology & neurosurgery 030304 developmental biology |
| Zdroj: | The Journal of Peptide Research. 61:47-57 |
| ISSN: | 1399-3011 1397-002X |
| DOI: | 10.1034/j.1399-3011.2003.21039.x |
| Popis: | Recently, it has been shown that mammalian PEBPs are implicated in several signalling pathways controlling the cellular cycle. In particular, during brain development, the N-terminal part of mammalian PEBP is specifically cleaved and the resulting 11 amino acid peptide stimulates the growth and activity of acetylcholinergic neurons. The crystallographic structure of bovine and human PEBPs has revealed that their N- and C-terminal parts are accessible and exposed to the solvent suggesting that they may be involved in specific interactions with cellular partners. We have chemically synthetized the two peptides corresponding to these terminal parts and studied their structure in solution by circular dichroism and NMR spectroscopies: both of them are well-structured. The N-terminal peptide is composed of a series of turns, leading to a hook conformation. The C-terminal peptide displays a globally helical conformation similar to that observed in the whole protein; it is characterized by an amphipatic feature with a hydrophobic cluster located on one side. These structural features enlighten previous fluorescence and monolayer experiments and give new insights on the roles of both PEBP termini. |
| Databáze: | OpenAIRE |
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