title: Conformation of retro-bombolitin I in aqueous solution containing surfactant micelles.
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.
authors: Department of Organic Chemistry, University of Padua, Italy.
authors: R
authors: R
authors: Battistutta
authors: A
authors: A
authors: Bisello
authors: S
authors: S
authors: Mammi
authors: E
authors: E
authors: Peggion
mesh_terms: D000595:Amino Acid Sequence; D001514:Bee Venoms / Q000737:chemistry*; D008823:Micelles; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D012996:Solutions; D013501:Surface-Active Agents; D014867:Water / Q000737:chemistry*
chemical_list: D001514:Bee Venoms; D008823:Micelles; D010455:Peptides; D012996:Solutions; D013501:Surface-Active Agents; C091613:retro-bombolitin I; D014867:Water