Defined SUMO Chemistry for Site-Specific Peptide Research
SUMOylation is a reversible post-translational modification in which a small ubiquitin-like modifier (SUMO) is attached through its C-terminal glycine to the ε-amino group of a selected lysine residue. In cells, the reaction is coordinated by the SAE1/SAE2 activating enzyme, the UBC9 conjugating enzyme, and SUMO E3 ligases.
SUMOylation can influence protein localization, transcription, chromatin organization, DNA-damage responses, stress signaling, and protein-protein interactions. Chemically defined SUMOylated peptides provide controlled materials for mechanistic studies, binding assays, antibody evaluation, and analytical method development.
Many SUMOylation events occur within the consensus motif
ΨKxE (where Ψ represents a hydrophobic residue, K is the modified lysine, x is any amino acid, and E is glutamic acid), although important non-consensus SUMOylation sites have also been identified.
Bio-Synthesis develops project-specific routes using Fmoc-based SPPS, orthogonal lysine protection, segment ligation, and chemoselective conjugation. Full SUMO conjugates, motif peptides, linkage mimics, and analytical standards are evaluated individually for sequence, topology, scale, purification, and release testing.
Biological Function
Supports studies of protein localization, transcription, DNA repair, chromatin organization, and cellular stress responses.
Synthetic Chemistry
Uses SPPS, orthogonal lysine protection, and chemoselective ligation to create site-defined SUMO constructs.
Research Applications
Provides defined materials for enzyme assays, binding studies, proteomics, biomarker work, and therapeutic research.