ArticleThe journal of physical chemistry. B2026
Quantifying the Sequence-Dependent Kinetic Protection of Reduced Heme in Peptide Amphiphile Nanofibers.
Article in The journal of physical chemistry. B, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Replicating the protective dielectric environment of natural cytochromes within synthetic assemblies is essential for the development of air-stable bioelectronics. We report a redox-triggered "supramolecular gate" in self-assembled peptide amphiphile (PA) nanofibers that provide significant kinetic protection to ferrous heme B under aerobic conditions. By systematically varying side-chain steric bulk and hydrophobicity in a series of c16HHX4K3 PAs, we identified a phenylalanine variant (c16HHFL3K3) that extends the ferrous lifetime to over five seconds. Using a comprehensive multicomponent kinetic model, we resolve an initial protection phase in the c16HHFL3K3 variant that is absent in smaller side-chain controls like alanine. Potentiometric titrations revealed massive redox hysteresis (ΔEm up to 305 mV), representing the mechanistic barrier required for the transition to a "locked" state. Circular dichroism spectra support this transition as a cooperative increase in superhelical twisting upon reduction. These findings establish sequence-specific design rules for stimulus-responsive "insulation" in peptide-based materials, enabling the protection of reactive redox centers in atmospheric environments.
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