Molecular Chaperone Therapy is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.
| Category | Protein homeostasis |
| Target | Misfolded proteins |
| Mechanism | Protein folding assistance |
| Diseases | AD, PD, HD, ALS, Prion diseases |
Molecular chaperones are proteins that assist in the proper folding, assembly, and stabilization of other proteins. In neurodegenerative diseases, pathological proteins (Aβ, tau, α-synuclein, huntingtin, TDP-43) misfold and aggregate, leading to cellular dysfunction and death.
Molecular chaperone therapy aims to:
Hsp90 Inhibitors
Hsp70 Inducers
Small Molecule Chaperones
Hsp40 (DNAJ Family)
Hsp110 Family
Amyloid-β Chaperones
Tau Chaperones
α-Synuclein Chaperones
LRRK2 Modulation
Mutant Huntingtin (mHTT)
Autophagy Enhancement
SOD1 Mutants
TDP-43 Pathology
PrP^Sc Targeting
| Compound | Target | Disease | Stage |
|---|---|---|---|
| Clioquinol | Aβ metal chelation | AD | Phase 2/3 |
| Trehalose | Autophagy induction | HD, AD, PD | Preclinical |
| TUDCA | Mitochondrial protection | HD, AD | Phase 2 |
| Geldanamycin | Hsp90 inhibition | ALS | Preclinical |
| 17-AAG | Hsp90 inhibition | PD | Phase 1 |
| Trial | Compound | Target | Phase | Status |
|---|---|---|---|---|
| NCT01739348 | Clioquinol | Aβ | Phase 2/3 | Completed |
| NCT03911128 | Trehalose | Autophagy | Phase 2 | Recruiting |
| NCT03854045 | TUDCA | Mitochondria | Phase 2 | Active |
| NCT04003116 | Bavachinin | Hsp90 | Phase 1 | Completed |
The study of Molecular Chaperone Therapy has evolved significantly over the past decades. Research in this area has revealed important insights into the underlying mechanisms of neurodegeneration and continues to drive therapeutic development.
Historical context and key discoveries in this field have shaped our current understanding and will continue to guide future research directions.
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