Back to Search
Start Over
Degradation of amyloid peptide aggregates by targeted singlet oxygen delivery from a benzothiazole functionalized naphthalene endoperoxide.
- Source :
-
Chemical communications (Cambridge, England) [Chem Commun (Camb)] 2022 Mar 18; Vol. 58 (23), pp. 3747-3750. Date of Electronic Publication: 2022 Mar 18. - Publication Year :
- 2022
-
Abstract
- Aggregate structures formed by amyloid-β (Aβ) are correlated with the progression of pathogenesis in Alzheimer's disease. Previous works have shown that photodynamic photosensitizers were effective in oxidatively degrading amyloid-β aggregates and thus decreasing their cytotoxicity under various conditions. In this work, we designed and synthesized a benzothiazole-naphthalene conjugate, with high level of structural analogy to Thioflavin T which is known to have high affinities for the amyloid peptide aggregates. The endoperoxide form (BZTN-O2) of this compound, which releases singlet oxygen with a half-life of 77 minutes at 37 °C, successfully inhibited and/or reversed amyloid aggregation. The endoperoxide is capable of singlet oxygen release without any need for light, and its charge-neutral form could allow blood-brain barrier (BBB) permeability. The therapeutic potential of such endoperoxide compounds with amyloid binding affinity is exciting.
Details
- Language :
- English
- ISSN :
- 1364-548X
- Volume :
- 58
- Issue :
- 23
- Database :
- MEDLINE
- Journal :
- Chemical communications (Cambridge, England)
- Publication Type :
- Academic Journal
- Accession number :
- 35072189
- Full Text :
- https://doi.org/10.1039/d1cc07133e