Polarized-Proton–Driven Emergence of Biological Chirality and Proto-Informational Imprints on PAN–[SNZ–Mg²⁺]P Interfaces

Biological homochirality is a defining signature of life, yet its physical origin remains unresolved. Here we propose and computationally test a minimal mechanism in which chirality emerges in silanized nanozyme systems subjected to weak global polarization, representing proton fluxes acting within geomagnetic fields. We show that chirality does not accumulate linearly with polarization; instead, it appears through a threshold-like symmetry-breaking process consistent with a second-order phase transition and is subsequently stabilized by interfacial imprinting, providing a physical basis for structural memory. When silanized [SNZ–Mg²⁺]P complexes interact with polyaromatic hydrocarbon (PAN) assemblies, repeated coordination and release events generate persistent interfacial imprints, which manifest geometrically as localized, asymmetric pockets. These imprints act as proto-functional units: they are chiral, spatially constrained, and capable of retaining structural biases across multiple interaction cycles. Quantitative analysis reveals that such imprint-derived pockets exhibit stochastic yet nonrandom nucleotide affinity, captured by significant mutual information between pocket affinity fingerprints and nucleotide preference under permutation controls (p ≈ 2 × 10⁻⁴). PAN assemblies play a dual role by acting as geometric templates and structural mutagens, reshaping the landscape of accessible imprints and biasing global nucleotide preference regimes (e.g., toward G-dominant states) while preserving proto-informational structure. Importantly, the imprints described here do not encode sequences or a genetic code; rather, they impose probabilistic constraints on molecular fixation, defining a pre-genetic form of information. Together, these results identify a physically plausible pathway from planetary-scale polarization phenomena to the emergence of chiral, proto-informational interfacial imprints, providing a constrained and testable bridge toward subsequent stages of peptide organization and genetic coding.