A Synthetic Zipper Peptide Motif Orchestrated via Co-operative Interplay of Hydrogen Bonding, Aromatic Stacking, and Backbone Chirality

Here,
we report on a new class of synthetic zipper peptide which assumes
its three-dimensional zipper-like structure via a co-operative interplay
of hydrogen bonding, aromatic stacking, and backbone chirality. Structural
studies carried out in both solid- and solution-state confirmed the
zipper-like structural architecture assumed by the synthetic peptide
which makes use of unusually remote inter-residual hydrogen-bonding
and aromatic stacking interactions to attain its shape. The effect
of chirality modulation and the extent of noncovalent forces in the
structure stabilization have also been comprehensively explored via
single-crystal X-ray diffraction and solution-state NMR studies. The
results highlight the utility of noncovalent forces in engineering
complex synthetic molecules with intriguing structural architectures.

本研究报道了一类新型合成拉链肽（synthetic zipper peptide），该肽通过氢键作用、芳香堆积与主链手性的协同互作，形成三维拉链状结构。针对该合成肽的结构研究在固态与溶液态下均得以开展，结果证实其确实呈现出拉链状结构架构——该肽借助罕见的跨残基远程氢键作用与芳香堆积相互作用，得以形成目标空间构象。本研究还通过单晶X射线衍射（single-crystal X-ray diffraction）与溶液态核磁共振（solution-state NMR）实验，全面探究了手性调控效应以及非共价作用力在结构稳定过程中的作用程度。研究结果凸显了非共价作用力在构建具有精妙结构特征的复杂合成分子中的应用价值。