title: Tuning micelles of a bioactive heptapeptide biosurfactant via extrinsically induced conformational transition of surfactin assembly.
abstract: We have studied the effects of extrinsic environmental conditions on the conformation of surfactin, a heptapeptide biosurfactant from Bacillus subtilis, in aqueous solutions. It has been made clear that temperature, pH, Ca2+ ions and the synthetic nonionic surfactant hepta-ethylene glycol (C12E7) affect the conformation of surfactin in aqueous solutions. The beta-sheet formation reached a maximum at 40 degrees C both in presence and absence of (C12E7) and the nonionic surfactant enhances the beta-sheet formation even at 25 degrees C. Ca2 + induced the formation of alpha-helices and caused this transition at 0.3 mM with surfactin monomers or at 0.5 mM with surfactin micelles, but above these transition concentrations of Ca2+ beta-sheets were observed. In micellar solution the beta-sheet structure was stabilized at pH values below 7 or upon addition of Ca2+ in concentrations above 0.5 mM. Our results indicated that the bioactive conformation of surfactin is most likely the beta-sheets when the molecules are assembled in micelles. The beta-sheet structure in micelles could be retained by tuning the micelles. Surfactin micelles could be tuned in the bioactive conformation by manipulating pH, temperature, Ca2+ or (C12E7) concentrations in surfactin solutions. Our results strongly indicated that Ca2+ and other molecules (such as C12E7) may function as directing templates in the assembly and conformation of surfactin in micelles. Thus, we suggest environmental manipulation and template-aided micellation (TAM) as a new approach for preparing predesigned micelles, microemulsions or micro-spheres for specific application purposes.
authors.affiliation: School of Science and Technology (HIS), Ullandhaug, Stavanger, Norway.
authors.forename: M
authors.initials: M
authors.lastname: Osman
authors.forename: H
authors.initials: H
authors.lastname: Høiland
authors.forename: H
authors.initials: H
authors.lastname: Holmsen
authors.forename: Y
authors.initials: Y
authors.lastname: Ishigami
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000187:drug effects; D002118:Calcium / Q000494:pharmacology; D002942:Circular Dichroism; D005026:Ethylene Glycols / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D055666:Lipopeptides; D008823:Micelles; D010456:Peptides, Cyclic / Q000737:chemistry; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D013501:Surface-Active Agents / Q000737:chemistry / Q000494:pharmacology; D013696:Temperature
chemical_list: D001426:Bacterial Proteins; D005026:Ethylene Glycols; D055666:Lipopeptides; D008823:Micelles; D010456:Peptides, Cyclic; D013501:Surface-Active Agents; C009365:surfactin peptide; D002118:Calcium