Sequence-selective recognition of peptides within the single binding pocket of a self-assembled coordination cage.
Sequence-selective recognition of peptides within the single binding pocket of a self-assembled coordination cage.
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DOI：
10.1021/ja044782y
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发表时间：
2005-03
影响因子：
15
通讯作者：
S. Tashiro;Masahide Tominaga;M. Kawano;B. Therrien;T. Ozeki;M. Fujita
中科院分区：
文献类型：
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作者：
S. Tashiro;Masahide Tominaga;M. Kawano;B. Therrien;T. Ozeki;M. Fujita
自组装Pd6L4配位笼的单结合袋以高度序列选择性的方式识别寡肽。特别是，Trp-Trp-Ala序列与空腔紧密结合（Ka >/=106 M-1）。具有相同残基但序列不同的三肽（即Trp-Ala-Trp和Ala-Trp-Trp）的亲和力要差得多。即使是残基具有芳香-芳香-脂肪族序列的单突变三肽（例如，Trp-Trp-Gly和trp - tyr1 - ala）也不能有效识别。x射线分析和核磁共振表明，Trp-Trp-Ala序列的所有残基都通过CH-pi和pi-pi相互作用与笼相互作用。
The single binding pocket of a self-assembled Pd6L4 coordination cage recognizes oligopeptides in a highly sequence-selective fashion. In particular, the Trp-Trp-Ala sequence is strongly bound by the cavity (Ka >/=106 M-1). Tripeptides possessing the same residues but in different sequences (i.e., Trp-Ala-Trp and Ala-Trp-Trp) show much poorer affinity. Even singly mutated tripeptides with aromatic-aromatic-aliphatic sequences of the residues (e.g., Trp-Trp-Gly and Trp-Tyr-Ala) are not recognized efficiently. X-ray analysis and NMR reveal that all residues of the Trp-Trp-Ala sequence cooperatively interact with the cage via CH-pi and pi-pi interactions.