Conformational flexibility of the hormonal peptide bombesin and its interaction with lipids
Cavatorta, P.; Farruggia, G.; Masotti, L.; Sartor, G.; Szabo, A.G.
Biochemical and Biophysical Research Communications 141(1): 99-105
1986
ISSN/ISBN: 0006-291X PMID: 3801011 Document Number: 270069
The conformational flexibility of the tetradecapeptide hormone bombesin has been studied using circular dichronism 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.