Conformational flexibility of the hormonal peptide bombesin and its interaction with lipids |
| |
Authors: | P Cavatorta G Farruggia L Masotti G Sartor A G Szabo |
| |
Affiliation: | 15. Institute of Biological Chemistry, University of Parma, 43100 Parma, Italy;4. Division of Biological Sciences, National Research Council, Ottawa, Canada, K1A OR6 |
| |
Abstract: | The conformational flexibility of the tetradecapeptide hormone bombesin has been studied using circular dichroism and fluorescence of its single tryptophan residue. The spectral changes observed indicate that the peptide changed from a random flexible coil in solution to a helical structure in lysolecithin micelles and dimyristoylphosphatidylserine vesicles. The tryptophan residue in the lipid complexes was located in a hydrophobic environment. The interaction with lipids was shown to involve both hydrophobic and electrostatic forces. |
| |
Keywords: | |
本文献已被 ScienceDirect 等数据库收录! |
|