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Metal-Peptide Torus Knots from Flexible Short Peptides
Chem ( IF 19.1 ) Pub Date : 2020-01-02 , DOI: 10.1016/j.chempr.2019.12.009
Yuuki Inomata , Tomohisa Sawada , Makoto Fujita

Entanglements of strings are regularly encountered on the macroscale yet rarely utilized in nanoscale construction. Here, we report highly entangled peptide-mimic structures created through folding and assembly of silver(I) ions and a triglycine ligand (L). The highly flexible triglycine strand assembled into a septafoil knot ([Ag⋅L]7) and its eight-crossing link analog ([Ag⋅L]8), both of which were formed for the first time by chemical synthesis. The two structures result from circular oligomerization of the same 1-crossing Ag⋅L motif. We also obtained poly[n]catenane [Ag⋅L]n from a topologically isomeric 2-crossing motif. Our observations reveal that dynamic linkages of short peptides enable easy access to knotted structures, which are restricted in protein structures because of the entropic (and/or kinetic) disadvantage of self-threading processes in long peptide chains, with remarkable stereoselectivity in the self-assembly process.



中文翻译:

柔性短肽的金属肽环结

字符串经常在宏观上遇到缠结,但很少用于纳米级构造中。在这里,我们报告高度折叠的肽模拟结构,通过折叠和组装银(I)离子和三甘氨酸配体(L)产生。高柔性的三甘氨酸链组装成七叶形结([Ag⋅L] 7)和它的八个交叉连接类似物([Ag⋅L] 8),两者都是通过化学合成首次形成的。这两个结构是由相同的1个交联的Ag⋅L基序的圆形低聚产生的。我们还获得了聚[ n ] catenane [Ag⋅L] n来自拓扑异构的2交点基序。我们的观察结果表明,短肽的动态键合使得易于进入打结的结构,而这种结构由于长肽链中自穿线过程的熵(和/或动力学)劣势而在蛋白质结构中受到限制,并且在自身结构中具有显着的立体选择性。组装过程。

更新日期:2020-01-02
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