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Can molecular dynamics facilitate the design of protein–protein-interaction inhibitors?

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The design of effective inhibitors of protein–protein interactions is challenging. In a new study, thermal fluctuation of protein structure was simulated to identify small-molecule candidates that inhibit protein–protein interactions. The application of this technique to other protein–protein interactions might facilitate the replacement of biologic agents with orally available small-molecule drugs.

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Authors and Affiliations

  1. Department of Pharmacy, The University of Tokyo Hospital, Faculty of Medicine, The University of Tokyo, Tokyo, Japan

    Masashi Honma & Hiroshi Suzuki

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  1. Masashi Honma
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  2. Hiroshi Suzuki
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Correspondence to Hiroshi Suzuki.

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The authors declare no competing interests.

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Honma, M., Suzuki, H. Can molecular dynamics facilitate the design of protein–protein-interaction inhibitors?. Nat Rev Rheumatol 19, 8–9 (2023). https://doi.org/10.1038/s41584-022-00877-2

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