Heat Shock Proteins (HSPs)

Heat Shock Proteins (HSPs) designate a family of molecular chaperones that protect cells under stress by assisting protein folding, preventing aggregation, and supporting degradation of misfolded proteins. These proteins are upregulated in response to heat, oxidative stress, inflammation, and other cellular insults. HSPs play roles in immune signalling, antigen presentation, and regulation of apoptosis, making them relevant in multiple disease contexts.

The biopharmaceutical industry investigates HSPs as therapeutic targets and biomarkers due to their involvement in tumour survival and resistance mechanisms. Cancer cells often exploit HSPs to stabilise oncogenic proteins, making HSP inhibitors attractive strategies for disrupting tumour viability. Drug discovery programmes evaluate HSP90 and related targets, though development must balance anti-tumour effects with potential toxicity in normal tissues. HSP expression also serves as a stress indicator in cell culture manufacturing, informing process optimisation and stability risk assessment. As biologics and complex modalities increase, understanding chaperone biology continues supporting both therapeutic innovation and manufacturing robustness.