Proteotyping rare amyloidosis disease by photocatalytic proteomics profiling

we present a photocatalytic proteomic method, named Amyloid-ID, as a quantitative approach to identify the composition of amyloid deposits for clinical proteotyping of amyloidosis diseases. Amyloid-ID is enabled by a photosensitized probe analogous to the pan-amyloid sensor Thioflavin T. We show this probe photocatalyzes gradient protein labeling originated from amyloid deposits and enriches them from tissue in a spatially-resolved manner. Next, we exemplify its application in proteotyping the pathogenic protein of the rare Laryngeal Amyloidosis (LA).