Center for Bio-Responsive Assembly and Department of Chemistry, Seoul National University, Seoul 151-747, Korea.
J Am Chem Soc. 2012 Dec 19;134(50):20270-2. doi: 10.1021/ja3098756. Epub 2012 Nov 28.
Effective stabilization of short peptide chains into a helical structure has been a challenge in the fields of chemistry and biology. Here we report a novel method for α-helix stabilization of short peptides through their confinement in a cyclic architecture. We synthesized block peptides based on a short peptide and a flexible linker as linear precursors. Subsequent cyclization of the peptide precursors resulted in a conformational change of the peptide unit from a random coil to an α-helix. The incorporation of hydrophobic residues into the peptide unit led to a facially amphiphilic conformation of the molecular cycle. The resulting amphiphilic peptide self-assembled into undulated nanofibers through the directional assembly of small oblate micelles.
将短肽链有效地稳定成螺旋结构一直是化学和生物学领域的一个挑战。在这里，我们报告了一种通过将短肽约束在环状结构中来稳定α-螺旋的新方法。我们合成了基于短肽和柔性接头的嵌段肽作为线性前体。随后，肽前体的环化导致肽单元的构象从无规卷曲转变为α-螺旋。将疏水性残基引入肽单元导致分子环呈现面两亲性构象。所得两亲性肽通过小的扁长形胶束的定向组装自组装成波状纳米纤维。
