Design of Boron-Based Peptidomimetics Leads to Potent Inhibitors of Human ClpP and ClpXP

03 December 2018, Version 1
This content is a preprint and has not undergone peer review at the time of posting.


Boronic acids have attracted the attention of synthetic and medicinal chemists due to boron’s ability to modulate enzyme function. Recently, we demonstrated that boron-containing amphoteric building blocks facilitate the discovery of bioactive aminoboronic acids. Herein, we have augmented this capability with a de novo library design and virtural screening platform modified for covalent ligands. This technique has allowed us to rapidly design and identify a series of α-aminoboronic acids as the first inhibitors of human ClpXP, which is responsible for the degradation of misfolded proteins.


Aminoboronic acids
Ugi Reaction
Organoboron reagents
Human ClpP
Human ClpXP
Covalent ligand virtual screening
User-designed virtual library

Supplementary materials

Design of boron-peptidomimetics leads to potent inhibitors of human ClpP and ClpXP


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