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Conformation of bombesin in buffer and in the presence of lysolecithin micelles: Nmr, CD, and fluorescence studies

✍ Scribed by P. Cavatorta; A. Spisni; A. G. Szabo; G. Farruggia; L. Franzoni; L. Masotti

Publisher
Wiley (John Wiley & Sons)
Year
1989
Tongue
English
Weight
879 KB
Volume
28
Category
Article
ISSN
0006-3525

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✦ Synopsis

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Synopsis

The conformation of the tetradecapeptide hormone bornbesin has been studied in buffer and in the presence of lysolecithin mides, using static and dynamic fluorescence, CD, and one and two-dimensional nmr. The reaults obtained show that in buffer bornbesin is present in an extended flexible chain, with no evidence for any ordered secondary structure. A marked change in the CD spectrum is observed changing from buffer to the lipid suspension. Concomitantly, the 'H-nmr spectrum of bornbesin, in a 4 0 lipid dispersion, shows the persistence of resonances due to exchangeable protons and in similar conditions the fluorescence intensity increases. We think therefore that these results strongly support the hypothesis that bornbesin interacts with the lipid phase, assuming ordered secondary structure. Finally, the marked dependence of tryptophan fluorescence quantum efficiency and order parameter from the hormone concentration in the presence of lysolecithin but not in buffer leads to the conclusion that bornbesin can associate into the lipid matrix.

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