Rational Design and Synthesis of Right-Handed d-Sulfono-γ-AApeptide Helical Foldamers as Potent Inhibitors of Protein-Protein Interactions.
Rational Design and Synthesis of Right-Handed d-Sulfono-γ-AApeptide Helical Foldamers as Potent Inhibitors of Protein-Protein Interactions.
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DOI：
10.1021/acs.joc.0c00996
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发表时间：
2020-08-21
期刊：
影响因子：
--
通讯作者：
Cai J
中科院分区：
文献类型：
--
作者：
Sang P;Shi Y;Higbee P;Wang M;Abdulkadir S;Lu J;Daughdrill G;Chen J;Cai J
Novel unprecedented helical foldamers have been effectively designed and synthesized. The homogeneous right-handed d-sulfono-γ-AApeptides represent a new generation of unnatural helical peptidomimetics, which have similar folding conformation to α-peptides, making them an ideal molecular scaffold to design α-helical mimetics. As demonstrated with p53-MDM2 PPI as a model application, the right-handed d-sulfono-γ-AApeptides reveal much-enhanced binding affinity compared to the p53 peptide. The design of d-sulfono-γ-AApeptides may provide a new and alternative strategy to modulate protein–protein interactions.
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DOI：
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发表时间：
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影响因子：
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DOI：
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影响因子：
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