Therapeutic applications of heat shock proteins and molecular chaperones

Molecular chaperones are stress and heat shock proteins (Hsps) having important characteristics associated with stabilisation of the functional conformation of proteins and protection against cellular toxicity, Hsp expression is enhanced in response to stress that can influence post-translational modification and denaturation of proteins. In the presence of Hsp, protein unfolding and aggregation in response to denaturing conditions is inhibited. Hsps support normal folding of partially folded proteins during biosynthesis. in the presence of endogenous Hsp there is increased cellular tolerance to thermal stress, ischaemia, oxidation and other adverse conditions that can modify protein conformation and produce partially unfolded states resulting in dysfunctional aggregates. The immunogenicity of Hsp bound antigenic peptides is enhanced. Each functional characteristic of Hsp is associated with protection against abnormal, stress related conditions in which therapeutic applications involving Hsp are under development. The current patent record indicates several therapeutic areas that are being actively pursued.