title: Structure, stability, and hydration of a polypeptide in AOT reverse micelles.
abstract: In this communication, we provide theoretical evidence that the folded structure of a simple peptide, alanine zwitterionic octapeptide, or A8, unstable in solution, becomes stable in a reverse micelle (RM) of appropriate size. Our molecular dynamics simulations were carried out for realistic models of sodium 2-ethylhexylsulfosuccinate RM in isooctane, simulated for an extended period of time. For the RM of the smaller size, we find that a helical structure is stable for the whole length of the simulation. On the contrary, the peptide very quickly takes an extended structure in larger micelles.
authors.affiliation: Commissariat à l'Energie Atomique, DSV-DBJC-SBFM, Centre d'Etudes, Saclay, Gif-sur-Yvette, France.
authors.forename: Stéphane
authors.initials: S
authors.lastname: Abel
authors.forename: Marcel
authors.initials: M
authors.lastname: Waks
authors.forename: Wladimir
authors.initials: W
authors.lastname: Urbach
authors.forename: Massimo
authors.initials: M
authors.lastname: Marchi
mesh_terms: D004143:Dioctyl Sulfosuccinic Acid / Q000737:chemistry*; D008823:Micelles; D009842:Oligopeptides / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013501:Surface-Active Agents / Q000737:chemistry*; D014867:Water / Q000737:chemistry
chemical_list: D008823:Micelles; D009842:Oligopeptides; D010455:Peptides; D013501:Surface-Active Agents; D014867:Water; D004143:Dioctyl Sulfosuccinic Acid; C019529:polyalanine