CARs-DB

CARs-DB catalogs cryptic amyloidogenic regions (CARs) within intrinsically disordered proteins (IDPs) to enable analysis of their prevalence, physicochemical properties, and associations with protein function and disease.

Key Features:

• Identification of CARs: Precomputed predictions of CARs are provided for intrinsically disordered proteins sourced from the DisProt database.
• Physicochemical properties: CARs are solvent-exposed, more polar, and display milder aggregation potential compared to conventional amyloid regions in globular proteins.
• Database content: The dataset comprises over 8,900 unique CARs identified across 1,711 intrinsically disordered regions (IDRs).
• Functional and pathological relevance: CARs are linked to disordered-mediated protein–protein interactions and to pathological contexts including cancer and Alzheimer's disease.
• Experimental validation: Two previously undescribed CARs extracted from the database were shown to exhibit full amyloidogenic potential.

Scientific Applications:

• IDP aggregation research: Enables study of amyloidogenic load and aggregation propensity within intrinsically disordered regions across proteomes.
• Protein interaction mapping: Facilitates identification of disordered interacting regions that may mediate functional binding via CARs.
• Disease mechanism studies: Supports investigation of the role of cryptic amyloidogenic sequences in protein misfolding diseases such as Alzheimer's disease and cancer.
• Therapeutic target discovery: Highlights previously unrecognized amyloidogenic sequences within IDRs as potential targets for intervention.

Methodology:

Precomputed CAR predictions were generated for intrinsically disordered proteins obtained from the DisProt database as part of proteome-wide analyses.