This open-access dataset presents Version 1 of the alpha B Crystallin (CRYAB) Degradome Foundation Atlas, a curated proteolytic peptide resource designed to advance translational research in protein aggregation myopathies and cardiomyopathies.The atlas integrates proteolytic fragments derived from human CRYAB, including wild-type and mutant (R120G) implicated in desmin-related myopathy and CRYAB associated cardiomyopathy [1]. By systematically mapping and annotating these cleavage products, the dataset provides a foundational framework for understanding proteostasis imbalance, aggregation dynamics, and degradation pathways in CRYAB linked disease(s).These data are particularly relevant for researchers studying molecular chaperone dysfunction, oxidative and reductive stress, and protein misfolding mechanisms in striated muscle and cardiac tissue. The atlas enables cross-referencing of peptide signatures with mutation type, tissue specificity, and experimental treatment response, supporting biomarker discovery, mechanistic modelling, and therapeutic target validation.Each peptide entry includes detailed information on cleavage position and biochemical properties. The dataset is distributed as a tab-delimited ASCII (.txt) file for seamless integration with bioinformatics and statistical workflows.ReproducibilityAll datasets can be regenerated using open-source tools (Python, BLAST, SAS). Fully documented scripts are available [3] to ensure transparency, reproducibility, and adaptability across computational environments, following the methodology described in [2].References[1] Rajasekaran NS, Connell P, Christians ES, Yan L-J, Taylor RP, Orosz A, et al.Human αB-Crystallin Mutation Causes Oxido-Reductive Stress and Protein Aggregation Cardiomyopathy in Mice.Cell. 2007;130(3):427–439. doi:10.1016/j.cell.2007.06.044[2] Petzold A. Proteolysis-Based Biomarker Repertoire of the Neurofilament Proteome.J Neurochem. 2025 Mar;169(3):e70023. doi:10.1111/jnc.70023. PMID: 40066701; PMCID: PMC11894590.[3] doi:10.5522/04/25689378