CONFORMATION OF RETRO-BOMBOLITIN-I IN AQUEOUS-SOLUTION CONTAINING SURFACTANT MICELLES

Citation
R. Battistutta et al., CONFORMATION OF RETRO-BOMBOLITIN-I IN AQUEOUS-SOLUTION CONTAINING SURFACTANT MICELLES, Biopolymers, 34(11), 1994, pp. 1535-1541
Citations number
24
Categorie Soggetti
Biology
Journal title
ISSN journal
00063525
Volume
34
Issue
11
Year of publication
1994
Pages
1535 - 1541
Database
ISI
SICI code
0006-3525(1994)34:11<1535:CORIAC>2.0.ZU;2-H
Abstract
Bombolitins are five naturally occurring heptadecapeptides acting at t he membrane level and able to increase the activity of phospholipase A (2). As for other peptides with similar function, the biological activ ity of bombolitins seems to be mainly due to their ability to form amp hipathic helical structures. We synthesized and tested the retro seque nce of bombolitin I (retro-bombolitin I). This peptide showed an activ ity similar to that of the natural sequence and was able to adopt a he lical structure in the presence of an amphipathic environment consisti ng of SDS micelles. The secondary structure of this peptide was fully characterized by CD and nmr spectroscopy. (C) 1994 John Wiley and Sons , Inc.