Amyloid-ID: photocatalytic profiling of amyloid deposits in Alzheimer's disease tissue.

ABSTRACT: Deposition of amyloid proteins and their associated interactome is a hallmark of Alzheimer's disease (AD) and other amyloidosis diseases, with their composition implying disease etiology. However, precise in-situ micro-dissection of amyloid deposits in AD brain tissue remains a challenge. In this work, we first divert the excited state energy of Thioflavin T from singlet fluorescence to triplet photocatalytic amyloid protein labeling through molecular engineering, while maintain its pan-amyloid binding affinity and selectivity. We further demonstrate that the amyloid labeling is catalyzed via type-I radical-based photosensitization with diverse residue modification sites. In female AD mouse brain tissue without homogenization, Amyloid-ID in-situ captures and profiles amyloid deposits, reli

SUBMITTER: Feng H 

PROVIDER: S-EPMC12864768 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature