PFEP as a Programmable Aqueous Interface for Peptide Dissolution, Purification, and Concentration

Peptide recovery can be lost before chromatography through incomplete wetting, pH-driven precipitation, interfacial adsorption, membrane binding, and concentration-induced self-association. This article defines PFEP as an ex situ aqueous-conditioning platform for creating a measured dissolution trajectory before purification and concentration. The mechanism is conventional physical chemistry: ionization, ionic strength, specific counterions, dissolved gases, redox impurities, surface charge, and mixing. No durable water memory is invoked. A synthetic mass-balance model predicts 21.4 mg/mL apparent soluble peptide and 95.8% total recovery for a programmed low-ionic-strength wetting–ionization–concentration sequence versus 7.8 mg/mL and 88.9% recovery for direct dissolution at the final pH. The figures are hypothetical. The study design requires complete recovery from supernatant, pellet, membranes, tubing, and vessels, plus chemically reconstructed controls. Article type: Process-theory article with synthetic mass-balance data. All numerical results labelled synthetic or modelled are hypothesis-illustration and planning outputs, not experimental measurements. No wet-laboratory experiment, 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.23382988
Primary Topic
Protein purification and stability
Type
preprint
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preprint

PFEP as a Programmable Aqueous Interface for Peptide Dissolution, Purification, and Concentration

Ilyan Kan
Zenodo (CERN European Organization for Nuclear Research)
Protein purification and stability
preprint

PFEP as a Programmable Aqueous Interface for Peptide Dissolution, Purification, and Concentration

Ilyan Kan
preprint en

Abstract

Peptide recovery can be lost before chromatography through incomplete wetting, pH-driven precipitation, interfacial adsorption, membrane binding, and concentration-induced self-association. This article defines PFEP as an ex situ aqueous-conditioning platform for creating a measured dissolution trajectory before purification and concentration. The mechanism is conventional physical chemistry: ionization, ionic strength, specific counterions, dissolved gases, redox impurities, surface charge, and mixing. No durable water memory is invoked. A synthetic mass-balance model predicts 21.4 mg/mL apparent soluble peptide and 95.8% total recovery for a programmed low-ionic-strength wetting–ionization–concentration sequence versus 7.8 mg/mL and 88.9% recovery for direct dissolution at the final pH. The figures are hypothetical. The study design requires complete recovery from supernatant, pellet, membranes, tubing, and vessels, plus chemically reconstructed controls. Article type: Process-theory article with synthetic mass-balance data. All numerical results labelled synthetic or modelled are hypothesis-illustration and planning outputs, not experimental measurements. No wet-laboratory experiment, validated process, clinical benefit, or shelf life is claimed.

Zenodo (CERN European Organization for Nuclear Research)
University of Toronto (CA)
Protein purification and stability
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