Horne W Seth, Yadav Maneesh K, Stout C David, Ghadiri M Reza
Departments of Chemistry, Molecular Biology, and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
J Am Chem Soc. 2004 Dec 1;126(47):15366-7. doi: 10.1021/ja0450408.
In this paper, we present 1,2,3-triazole epsilon2-amino acids incorporated as a dipeptide surrogate at three positions in the sequence of a known alpha-helical coiled coil. Biophysical characterization indicates that the modified peptides retain much of the helical structure of the parent sequence, and that the thermodynamic stability of the coiled coil depends on the position of the incorporation of the epsilon-residue. Crystal structures obtained for each peptide give insight into the chemical behavior and conformational preferences of the non-natural amino acid and show that the triazole ring can participate in the backbone hydrogen bonding of the alpha-helix as well as template an interhelical crossing between chains in the bundle.
在本文中,我们展示了将1,2,3 - 三氮唑ε2 - 氨基酸作为二肽类似物掺入已知α - 螺旋卷曲螺旋序列的三个位置。生物物理表征表明,修饰后的肽保留了母体序列的大部分螺旋结构,并且卷曲螺旋的热力学稳定性取决于ε - 残基掺入的位置。为每个肽获得的晶体结构深入了解了非天然氨基酸的化学行为和构象偏好,并表明三氮唑环可以参与α - 螺旋的主链氢键形成,以及在束状结构中模板化链间的螺旋间交叉。