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Targeting protein folding: A novel approach for the treatment of pathogenic bacteria
Journal article   Peer reviewed

Targeting protein folding: A novel approach for the treatment of pathogenic bacteria

N.J. Scheuplein, N.M. Bzdyl, E.A. Kibble, T. Lohr, U. Holzgrabe and M. Sarkar-Tyson
Journal of Medicinal Chemistry, Vol.63(22), pp.13355-13388
2020
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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.

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UN Sustainable Development Goals (SDGs)

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#3 Good Health and Well-Being

Source: InCites

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Collaboration types
Domestic collaboration
International collaboration
Citation topics
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
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