Heterocyclic peptide backbone modifications in an α-helical coiled coil
Heterocyclic peptide backbone modifications in an α-helical coiled coil
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DOI：
10.1021/ja0450408
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发表时间：
2004-12-01
影响因子：
15
通讯作者：
Ghadiri, MR
中科院分区：
文献类型：
--
作者：
Horne, WS;Yadav, MK;Ghadiri, MR
在本文中，我们提出了1，2，3-三唑ε2-氨基酸作为二肽替代品纳入在一个已知的α-螺旋卷曲螺旋序列的三个位置。生物物理表征表明，修饰的肽保留了亲本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-残基的掺入位置。获得的每种肽的晶体结构可以深入了解非天然氨基酸的化学行为和构象偏好，并表明三唑环可以参与α-螺旋的骨架氢键，以及模板束中链之间的螺旋间交叉。
In this paper, we present 1,2,3-triazole ε2-amino acids incorporated as a dipeptide surrogate at three positions in the sequence of a known α-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 ε-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 α-helix as well as template an interhelical crossing between chains in the bundle.