Abel Stéphane, Waks Marcel, Urbach Wladimir, Marchi Massimo
Commissariat à l'Energie Atomique, DSV-DBJC-SBFM, Centre d'Etudes, Saclay, Gif-sur-Yvette, France.
J Am Chem Soc. 2006 Jan 18;128(2):382-3. doi: 10.1021/ja053043u.
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.
在本通讯中，我们提供了理论证据，即一种简单肽（丙氨酸两性离子八肽，或A8）在溶液中不稳定的折叠结构，在适当大小的反胶束（RM）中变得稳定。我们对异辛烷中2-乙基己基磺基琥珀酸钠RM的真实模型进行了分子动力学模拟，并进行了较长时间的模拟。对于较小尺寸的RM，我们发现在整个模拟过程中螺旋结构都是稳定的。相反，该肽在较大的胶束中很快就会形成伸展结构。
