Conformation of retro-bombolitin I in aqueous solution containing surfactant micelles
β Scribed by Roberto Battistutta; Alessandro Bisello; Stefano Mammi; Evaristo Peggion
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1994
- Tongue
- English
- Weight
- 592 KB
- Volume
- 34
- Category
- Article
- ISSN
- 0006-3525
No coin nor oath required. For personal study only.
β¦ Synopsis
Abstract
Bombolitins are five naturally occurring heptadecapeptides acting at the membrane level and able to increase the activity of phospholipase A~2~. 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 bomβbolitin I (retroβbombolitin 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. Β© 1994 John Wiley & Sons, Inc.
π SIMILAR VOLUMES
The peptide toxin bombolitin III [B(III)], originally isolated from bumblebee venom, has been shown to undergo a concentration-dependent conformational change from a random structure to an alpha-helix induced by aggregation. The aggregation process and the consequent folding results from a delicate
Two nonionic surfactant dimers (gemini surfactants) of the dimethylene 1,2-bis(N-polyethyleneglycol dodecylamide) type and the corresponding surfactant monomers of the N-methyl, Npolyethyleneglycol dodecylamide type have been synthesized with an increasing number of ethyleneglycol (EG) units in the