Molecular Classification
Protein, Heat Shock Protein, Chaperonin
Other Names
Molecular Chaperone, Heat Shock Protein, Hsp60, Hsp70, BiP, GroEL/GroES, DnaK/DnaJ, NAC
Disease Roles
Neurodegenerative diseaseAlzheimer’s diseaseParkinson’s disease

Chaperone Protein Overview

Chaperone proteins, also known as molecular chaperones, are a diverse group of proteins that assist other proteins in achieving proper folding, assembly, and conformational maintenance. They play a crucial role in cellular homeostasis by preventing the aggregation of misfolded or partially folded polypeptides and facilitating their correct folding during or after synthesis. Malfunction or deficiency in molecular chaperones is implicated in several diseases characterized by protein misfolding/aggregation. They are indispensable guardians ensuring proteome integrity across all domains of life by guiding nascent chains toward functional three-dimensional structures while protecting cells from potentially toxic aggregates arising from misfolding events.

Mechanism of Action

Facilitates correct protein folding; prevents aggregation

Biological Functions

Protein folding
Protein assembly
Prevention of protein aggregation
Protein transport
Regulation of signal transduction
Protein quality control

Disease Associations

Neurodegenerative disease
Alzheimer’s disease
Parkinson’s disease
Huntington’s disease
Type 2 diabetes
Retinitis pigmentosa
Protein misfolding diseases

Safety Considerations

  • Off-target effects due to broad substrate specificity