PFEP for Retatrutide: A Mechanistically Bounded Hypothesis and Minimal Falsification Experiment
Retatrutide is a long, lipidated, linear peptide whose aqueous processing is expected to couple ionization, oligomerization, interfacial adsorption, and degradation. It contains no cysteine and therefore offers no direct disulfide-folding rationale for PFEP. This article states the narrow hypothesis that ex situ qualified fractions can improve dissolution and compounding reproducibility by programming pH-capacity and ionic trajectories before final formulation lock. A minimal 12-condition experiment compares PFEP, conventional titration, full chemical reconstruction, and deliberately aged fractions at two peptide concentrations and three ionic-strength regimes. Synthetic outputs predict 92.1% intact soluble monomer after 28 days at 40 °C for PFEP, 91.7% for chemical reconstruction, and 82.0% for direct compounding. The near-equality of PFEP and reconstruction is an intended result: it supports an engineering route but rejects unique electrochemical water claims. No retatrutide experiment or shelf life is reported. Article type: Hypothesis article and pre-specified proof-of-concept protocol with synthetic 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.
Authors
- Ilyan Kan (ORCID: https://orcid.org/0000-0002-7534-2537)
Institutions
- University of Toronto (CA)
Publication Details
- Journal
- Zenodo (CERN European Organization for Nuclear Research)
- Published
- 2026-10-15
- DOI
- https://doi.org/10.5281/zenodo.23383009
- Primary Topic
- Protein purification and stability
- Type
- preprint