Peptide-based molecules for the disruption of bacterial Hsp70 chaperones

Aweon Richards, Tania J. Lupoli

Research output: Contribution to journalReview articlepeer-review


DnaK is a chaperone that aids in nascent protein folding and the maintenance of proteome stability across bacteria. Due to the importance of DnaK in cellular proteostasis, there have been efforts to generate molecules that modulate its function. In nature, both protein substrates and antimicrobial peptides interact with DnaK. However, many of these ligands interact with other cellular machinery as well. Recent work has sought to modify these peptide scaffolds to create DnaK-selective and species-specific probes. Others have reported protein domain mimics of interaction partners to disrupt cellular DnaK function and high-throughput screening approaches to discover clinically-relevant peptidomimetics that inhibit DnaK. The described work provides a foundation for the design of new assays and molecules to regulate DnaK activity.

Original languageEnglish (US)
Article number102373
JournalCurrent Opinion in Chemical Biology
StatePublished - Oct 2023

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry


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