POS4-0429
Ice-Plane-Selective Binding of AFP-Mimetic Peptides Across Atomic-to-Macroscopic Length Scales
Topic
S4. Colloids, Interfaces, and Molecular Assemblies for Functional Soft Materials
When and Where
Sep 29, 2026
08:30 - 09:30
Room 301 (Grand Ballroom)
Session Chairs
Hae Jung SON
Boseok KANG
Presenter(s)
Minyoung Son (GIST)
Co-Author(s)
Abstract
Antifreeze proteins (AFPs) inhibit ice recrystallization by binding specific crystal planes, arresting ice growth at the molecular level. Despite this remarkable activity, AFPs are structurally complex and costly to produce, limiting their practical use as cryoprotectants. Short AFP-mimetic peptides offer a scalable alternative, yet how peptide molecular structure and supramolecular assembly govern ice-plane selectivity across multiple length scales remains unclear.
Here, we present short AFP-mimetic peptides with tunable, plane-selective ice binding, characterized through a multiscale framework spanning atomic to macroscopic length scales. Molecular dynamics simulations identify the atomic-level interactions and geometric complementarity that drive plane-selective adsorption. These simulations clarify how individual residues recognize specific ice crystal faces. TEM and cryo-TEM resolve the self-assembled nanostructures formed in aqueous conditions, linking supramolecular organization and peptide chirality to ice-binding behavior. Interfacial characterization further probes how these assemblies organize at the ice surface to mediate plane recognition. At the macroscopic scale, fluorescence-based ice-plane affinity (FIPA) analysis on single-crystal ice maps binding preferences across distinct crystal planes. This reveals sequence-dependent selectivity that shifts with peptide length.
Together, these results show that ice-plane selectivity and interfacial activity emerge from a structural hierarchy spanning atomic contacts, supramolecular assembly geometry, and macroscopic ice binding. All of these features are tunable through peptide sequence design. By directly correlating molecular and supramolecular structure with macroscopic ice-binding performance, this work establishes a molecular design framework for AFP-mimetic peptides and offers practical guidelines for developing next-generation peptide-based cryoprotectants.
Here, we present short AFP-mimetic peptides with tunable, plane-selective ice binding, characterized through a multiscale framework spanning atomic to macroscopic length scales. Molecular dynamics simulations identify the atomic-level interactions and geometric complementarity that drive plane-selective adsorption. These simulations clarify how individual residues recognize specific ice crystal faces. TEM and cryo-TEM resolve the self-assembled nanostructures formed in aqueous conditions, linking supramolecular organization and peptide chirality to ice-binding behavior. Interfacial characterization further probes how these assemblies organize at the ice surface to mediate plane recognition. At the macroscopic scale, fluorescence-based ice-plane affinity (FIPA) analysis on single-crystal ice maps binding preferences across distinct crystal planes. This reveals sequence-dependent selectivity that shifts with peptide length.
Together, these results show that ice-plane selectivity and interfacial activity emerge from a structural hierarchy spanning atomic contacts, supramolecular assembly geometry, and macroscopic ice binding. All of these features are tunable through peptide sequence design. By directly correlating molecular and supramolecular structure with macroscopic ice-binding performance, this work establishes a molecular design framework for AFP-mimetic peptides and offers practical guidelines for developing next-generation peptide-based cryoprotectants.
