Paired-Fraction Electrochemical Programming of Aqueous Peptide-Chain Assembly

Peptide-chain assembly in water is constrained by the competition between productive aminolysis or ligation and hydrolysis, enzyme deactivation, substrate precipitation, and time-dependent product cleavage. This paper formulates a target-independent version of paired-fraction electrochemical programming (PFEP) in which anodic and cathodic liquids are generated outside the reaction vessel, analytically released, and metered into an electrode-free ligation reactor. PFEP is not proposed to condense unactivated amino acids. Its proposed function is to impose a measured trajectory of acid-base capacity, ionic composition, and, where chemically justified, redox capacity around an established activated-donor or enzyme-catalysed bond-forming reaction. A kinetic model links pH-dependent aminolysis and hydrolysis to cumulative qualified fraction dose. Synthetic demonstration data predict an assay-corrected product yield of 74.8% for a programmed trajectory versus 62.1% for an optimized static comparator at equal substrate loading. These values are not measurements. A causal experiment, chemical-reconstruction control, power calculation, mass-balance requirement, and falsification rules are specified. Article type: Original theoretical research with synthetic model data and a prospective validation protocol. All numerical results labelled synthetic or modelled are hypothesis-illustration and planning outputs, not experimental measurements. No validated process, clinical benefit, or shelf life is claimed.

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Publication Details

Journal
Zenodo (CERN European Organization for Nuclear Research)
Published
2026-10-15
DOI
https://doi.org/10.5281/zenodo.23382953
Primary Topic
Chemical Synthesis and Analysis
Type
preprint
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Paired-Fraction Electrochemical Programming of Aqueous Peptide-Chain Assembly

Ilyan Kan
Zenodo (CERN European Organization for Nuclear Research)
Chemical Synthesis and Analysis
preprint

Paired-Fraction Electrochemical Programming of Aqueous Peptide-Chain Assembly

Ilyan Kan
preprint en

Abstract

Peptide-chain assembly in water is constrained by the competition between productive aminolysis or ligation and hydrolysis, enzyme deactivation, substrate precipitation, and time-dependent product cleavage. This paper formulates a target-independent version of paired-fraction electrochemical programming (PFEP) in which anodic and cathodic liquids are generated outside the reaction vessel, analytically released, and metered into an electrode-free ligation reactor. PFEP is not proposed to condense unactivated amino acids. Its proposed function is to impose a measured trajectory of acid-base capacity, ionic composition, and, where chemically justified, redox capacity around an established activated-donor or enzyme-catalysed bond-forming reaction. A kinetic model links pH-dependent aminolysis and hydrolysis to cumulative qualified fraction dose. Synthetic demonstration data predict an assay-corrected product yield of 74.8% for a programmed trajectory versus 62.1% for an optimized static comparator at equal substrate loading. These values are not measurements. A causal experiment, chemical-reconstruction control, power calculation, mass-balance requirement, and falsification rules are specified. Article type: Original theoretical research with synthetic model data and a prospective validation protocol. All numerical results labelled synthetic or modelled are hypothesis-illustration and planning outputs, not experimental measurements. No validated process, clinical benefit, or shelf life is claimed.

Zenodo (CERN European Organization for Nuclear Research)
University of Toronto (CA)
Chemical Synthesis and Analysis
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