Title:Are Hsp90 Inhibitors Good Candidates Against Covid-19?
Volume: 22
Issue: 3
Author(s): Carlos H. I. Ramos*Kehinde S. Ayinde
Affiliation:
- Institute of Chemistry, University of Campinas UNICAMP, Campinas SP, 13083-970,Brazil
Keywords:
Drug reposition, drug repurposing, Hsp90, Viral proteins, protein stabilization, protein folding, coronavirus,
covid-19.
Abstract: Drug reposition, or repurposing, has become a promising strategy in therapeutics due to
its advantages in several aspects of drug therapy. General drug development is expensive and can
take more than 10 years to go through the designing, development, and necessary approval steps.
However, established drugs have already overcome these steps and thus a potential candidate may
be already available decreasing the risks and costs involved. In case of viral diseases, virus invades
the cells of host organism and provoke biochemical changes in it that lead to tissue damage, alternations
in normal physiological functions and sometimes death. Inside the cell, the virus finds the
machinery necessary for its multiplication, as for instance the protein quality control system, which
involves chaperones and Hsps (heat shock proteins) that, in addition to physiological functions,
help in the stabilization of viral proteins. Recently, many inhibitors of Hsp90 have been developed
as therapeutic strategies against diseases such as the Hsp90 inhibitors used in anticancer therapy.
Several shreds of evidence indicate that these inhibitors can also be used as therapeutic strategies
against viruses. Therefore, since a drug treatment for COVID-19 is urgently needed, this review
aims to discuss the potential use of Hsp90 inhibitors in the treatment of this globally threatening
disease.
