Transglutaminases (TGs) are enzymes that catalyze post-translational modifications of glutamine residues in proteins, via the formation of isopeptide bonds, esterification and deamination. The reaction produces insoluble macromolecular complexes and protein aggregates. Within the TG family of enzyme, tissue-specific Transglutaminase-2 (TG2) expression is proven to be a clinical target for multiple types of cancer and neurodegenerative diseases, including Alzheimer's and Huntington's diseases. Inhibition of TG2, with a Cystamine-derived drug candidate (currently in phase-II clinical trial for Huntington's disease), has shown to have neuroprotective effects in models of neurodegeneration. Further, TG2 interacts with retinoblastoma protein (Rb