Abstract
Hsp90 is an evolutionarily conserved adenosine triphosphate-dependent molecular chaperone
and is one of the most abundant proteins in the cells (1–3 %). Hsp90 is induced when
a cell undergoes various types of environmental stresses such as heat, cold, or oxygen
deprivation. It is involved in the turnover, trafficking, and activity of client proteins,
including apoptotic factors, protein kinases, transcription factors, signaling proteins,
and a number of oncoproteins. Most of the Hsp90 client proteins are involved in cell
growth, differentiation, and survival, and include kinases, nuclear hormone receptors,
transcription factors, and other proteins associated with almost all the hallmarks
of cancer. Consistent with these diverse activities, genetic and biochemical studies
have demonstrated the implication of Hsp90 in a range of diseases, including cancer,
making this chaperone an interesting target for drug research.
During the last few decades, plant secondary metabolites have been studied as a major
source for lead compounds in drug discovery. Recently, several plant-derived small
molecules have been discovered exhibiting inhibitory activity towards Hsp90, such
as epigallocatechin gallate, gedunin, lentiginosine, celastrol, and deguelin. In this
work, an overview of plant secondary metabolites interfering with Hsp90 activities
is provided.
Key words
Hsp90 - Hsp90 inhibitors - plant molecules - client proteins
