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Conformation of retro-bombolitin I in aqueous solution containing surfactant micelles.

Authors :
Battistutta R
Bisello A
Mammi S
Peggion E
Source :
Biopolymers [Biopolymers] 1994 Nov; Vol. 34 (11), pp. 1535-41.
Publication Year :
1994

Abstract

Bombolitins are five naturally occurring heptadecapeptides acting at the membrane level and able to increase the activity of phospholipase A2. As for other peptides with similar function, the biological activity of bombolitins seems to be mainly due to their ability to form amphipathic helical structures. We synthesized and tested the retro sequence of bombolitin I (retro-bombolitin I). This peptide showed an activity similar to that of the natural sequence and was able to adopt a helical structure in the presence of an amphipathic environment consisting of SDS micelles. The secondary structure of this peptide was fully characterized by CD and nmr spectroscopy.

Details

Language :
English
ISSN :
0006-3525
Volume :
34
Issue :
11
Database :
MEDLINE
Journal :
Biopolymers
Publication Type :
Academic Journal
Accession number :
7827265
Full Text :
https://doi.org/10.1002/bip.360341111