Deposition of amyloid proteins and their associated interactome (amyloidome) is a pathological hallmark of Alzheimer’s disease (AD) as well as other neurodegenerative diseases. However, achieving precise and targeted identification of the amyloidome has remained a significant challenge. To address this, we presents a photochemical proteomic strategy (namely Amyloid-ID) to profile the protein composition of amyloid deposits in AD mouse hippocampus sections. This strategy involves the development of a photosensitized Thioflavin T derivative to perform selective photocatalytic labeling of amyloids and their adjacent interactome using nucleophilic substrates. The probe is engineered to divert excited state energy from singlet fluorescence to triplet photosensitized labeling while maintaining its pan-amyloid binding affinity and selectivity. Tandem mass spectrometry (LC-MS/MS) and photochemical characterizations reveal diverse residue modification sites and bioconjugation mechanisms via type-I radical based photosensitization. In an AD mouse model (3×Tg), we demonstrate the Amyloid-ID technique in chemoproteomic profiling of amyloidome composition. The technical feasibility is validated by immunofluorescence co-localization of identified hits and proteomic alignments with reported amyloidome datasets. Finally, we employ this technique to examine amyloidomic variations among three commonly used neurodegenerative mouse models (3×Tg, rTg4510, and APP/PS1). Overall, this work exemplifies a chemical extension of the proximity labeling concept, showcasing a powerful strategy for the targeted identification of amyloidosis-related proteins in neurodegenerative diseases.