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Protein-protein inhibitor designed de-novo to target the MEEVD region on the C-terminus of Hsp90 and block co-chaperone activity

Abstract

Protein-protein interactions control all cellular functions. Presented is the first de-novo designed protein-protein inhibitor that targets the C-terminus of Heat shock protein 90 (Hsp90) and blocks co-chaperones from binding. Compound LB76, which was created from an Hsp90 co-chaperone, selectively pulls down Hsp90 from cell lysates, binds to Hsp90’s C-terminal domain, and blocks the interactions between Hsp90 and TPR-containing co-chaperones. Through these interactions, LB76 inhibits the protein-folding function of Hsp90. Blocking these protein-protein interactions between Hsp90 and C-terminal co-chaperones regulate the cell’s entire protein-folding machinery.

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Publication details

The article was received on 19 Sep 2018, accepted on 29 Nov 2018 and first published on 03 Dec 2018


Article type: Communication
DOI: 10.1039/C8CC07576J
Citation: Chem. Commun., 2018, Accepted Manuscript
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    Protein-protein inhibitor designed de-novo to target the MEEVD region on the C-terminus of Hsp90 and block co-chaperone activity

    M. N. Rahimi and S. R. McAlpine, Chem. Commun., 2018, Accepted Manuscript , DOI: 10.1039/C8CC07576J

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