Precise Control Over Kinetics Assembly of Potent Antifreeze Peptide from Ice‐Templated Strategy

Precise kinetic control over peptide assembly into functional nanostructures remains a major challenging. Herein, we report a novel ice‐templated assembly strategy driven by programmed ice recrystallization, which enables ultrafast, kinetically tunable fabrication of peptides into well‐defined nanofibers with precisely controllable dimensions. The nanostructure size can be quantitatively correlated with recrystallization parameters, including temperature and annealing time, providing a direct route to regulate assembly kinetics. The 4‐mercaptobenzoic acid‐modified threonine pentamer (MT5) exhibits exceptional ice recrystallization inhibition (IRI) activity, originating from the aligned threonine residues that afford enhanced ice‐binding affinity. Importantly, MT5 nanofibers enabled reduced‐DMSO cell cryopreservation, maintaining post‐thaw cell viability with 5% (v/v) DMSO at a level comparable to the standard 10% (v/v) DMSO formulation. Molecular dynamics simulations revealed that the neighboring threonine on MT5 match the spacing of one ice lattice on the primary prism plane. This ice‐templated method breaks through the bottlenecks of conventional peptide assembly, offers a versatile and programmable platform for rapid fabrication of functional nanostructures, and unlocks new routes for the rational design of high‐performance antifreeze materials.