Paired-Fraction Electrochemical Programming of Enzymatic Tripeptide Synthesis

Z-Pro-Leu-Gly-NH2 is proposed as a three-residue model for testing whether paired-fraction electrochemical programming (PFEP) can control an enzyme-catalysed coupling without exposing substrates or catalyst to an electrode. Published thermolysin and alpha-chymotrypsin studies establish that the product can be made enzymatically and that yield depends on pH, salt, solvent, substrate ratio, enzyme loading, and reaction time. PFEP therefore enters as a process-control layer, not as a new bond-forming mechanism. Qualified anodic and cathodic fractions are dosed to regulate the enzyme-compatible pH trajectory and to terminate the synthesis-dominant interval before donor hydrolysis or product cleavage dominates. The proposed experiment compares PFEP with an optimized static process, a conventional pH-stat, premixed fractions, each fraction alone, and a chemically reconstructed trajectory. LC methods must separately quantify donor, acceptor, dipeptide intermediates, tripeptide, and hydrolysis products. The theory is rejected if electrochemical origin adds no reproducible advantage after chemical matching. No experimental result is claimed. Article type: Perspective, mechanistic hypothesis, and experimental framework. No experimental peptide yield, potency, clinical effect, or shelf-life evidence is reported.