Structure, stability, and hydration of a polypeptide in AOT reverse micelles.
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.
Abel
Stéphane
S
Commissariat à l'Energie Atomique, DSV-DBJC-SBFM, Centre d'Etudes, Saclay, Gif-sur-Yvette, France.
Waks
Marcel
M
Urbach
Wladimir
W
Marchi
Massimo
M
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
D008823:Micelles; D009842:Oligopeptides; D010455:Peptides; D013501:Surface-Active Agents; D014867:Water; D004143:Dioctyl Sulfosuccinic Acid; C019529:polyalanine