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Hsp90 as Drug Target Against Bacterial and Fungal Infections

Author(s):

Zehra Edis*, Samir Haj Bloukh, Mohammad Waseemul Islam and Sabreena Ait Gacem   Pages 1 - 16 ( 16 )

Abstract:


Heat shock protein 90 (Hsp90) is a molecular chaperone protein, which is essential for cellular survival and plays a vital role in promoting proper protein folding, preventing, misfolding and restoring three-dimensional protein structure, supportive in cellular hostile environment. These chaperones are important proteins that help to promote cell survival in response of the variety of environmental stresses of the host. In recent years, Hsp gained interest in cancer therapy and as drug target against microbial infections. Emerging antimicrobial resistance poses a threat to humankind. Increasing antibiotic resistance, especially by Gram-negative pathogens requires development of drugs, which target molecular chaperones in order to inhibit the growth of dangerous microorganisms. Hsp90 family proteins of pathogens producing Hsp90 inhibitor antibiotics reveal mechanisms leading to drug resistance through amino acid changes in the ADP/ATP-binding site of hsp90. For this review we used the databases and websites PubMed, SciFinder, Scopus, ProQuest, Google and Google Scholar. The current review discusses the recent progress in the development and testing of Hsp90 inhibitors for bacterial as well as fungal infections and how these inhibitors are being used for clinical trials.

Keywords:

Hsp90, Chaperone, Protein, Antibiotic, Resistance, Cancer, Bacteria

Affiliation:

Ajman University, College of Pharmacy-Pharmaceutical Sciences, Ajman-Al Jurf, Ajman University, College of Pharmacy-Pharmaceutical Sciences, Ajman-Al Jurf, Ajman University, College of Pharmacy-Pharmaceutical Sciences, Ajman-Al Jurf, Ajman University, College of Pharmacy-Pharmaceutical Sciences, Ajman-Al Jurf



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