Journal article
Targeting protein folding: A novel approach for the treatment of pathogenic bacteria
Journal of Medicinal Chemistry, Vol.63(22), pp.13355-13388
2020
Abstract
Infectious diseases are a major cause of morbidity and mortality worldwide, exacerbated by increasing antibiotic resistance in many bacterial species. The development of drugs with new modes of action is essential. A leading strategy is antivirulence, with the aim to target bacterial proteins that are important in disease causation and progression but do not affect growth, resulting in reduced selective pressure for resistance. Immunophilins, a superfamily of peptidyl-prolyl cis–trans isomerase (PPIase) enzymes have been shown to be important for virulence in a broad-spectrum of pathogenic bacteria. This Perspective will provide an overview of the recent advances made in understanding the role of each immunophilin family, cyclophilins, FK506 binding proteins (FKBPs), and parvulins in bacteria. Inhibitor design and medicinal chemistry strategies for development of novel drugs against bacterial FKBPs will be discussed. Furthermore, drugs against human cyclophilins and parvulins will be reviewed in their current indication as antiviral and anticancer therapies.
Details
- Title
- Targeting protein folding: A novel approach for the treatment of pathogenic bacteria
- Authors/Creators
- N.J. Scheuplein (Author/Creator)N.M. Bzdyl (Author/Creator)E.A. Kibble (Author/Creator)T. Lohr (Author/Creator)U. Holzgrabe (Author/Creator)M. Sarkar-Tyson (Author/Creator)
- Publication Details
- Journal of Medicinal Chemistry, Vol.63(22), pp.13355-13388
- Publisher
- American Chemical Society
- Identifiers
- 991005541686007891
- Copyright
- © 2020 American Chemical Society
- Murdoch Affiliation
- School of Veterinary and Life Sciences
- Language
- English
- Resource Type
- Journal article
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- 1 Clinical & Life Sciences
- 1.157 Organ Donation & Transplantation
- 1.157.504 Transplant Immunosuppression
- Web Of Science research areas
- Chemistry, Medicinal
- ESI research areas
- Chemistry