POS4-1063
Rational Design of Short Peptide Mimics for Dual-Functional Cryoprotection
Topic
S4. Colloids, Interfaces, and Molecular Assemblies for Functional Soft Materials
When and Where
Oct 1, 2026
08:30 - 09:30
Room 301 (Grand Ballroom)
Session Chairs
Jinkee HONG
Ki Su KIM
Presenter(s)
YINGJIE BU (Gwangju Institute of Science and Technology)
Co-Author(s)
Abstract
The clinical translation of natural ice-binding proteins is hindered by their high cost and synthetic complexity. Short peptides offer a scalable alternative, yet engineering them to combine ice control with cell protection remains challenging. Here, we report a de novo design strategy for short peptide mimics that achieve dual-functional cryoprotection through combined supramolecular and sequence-level engineering. For the ice-control function, spectroscopic analyses and cryogenic transmission electron microscopy (cryo-TEM) reveal β-sheet-rich nanostructures stabilized by hydrogen bonding, in which the assembled state geometrically aligns hydrogen-bonding residues to match the ice-crystal lattice, enabling robust ice-recrystallization inhibition and marked suppression of ice-grain growth relative to controls. For the cell-protective function, position-specific design rules introduce amphiphilic charge segregation that drives electrostatic and hydrophobic interactions with cell membranes, modulating water permeability during freezing and improving post-thaw cell viability over untreated controls. Together, these results show that precise supramolecular and sequence design provides a scalable short-peptide platform uniting ice control and membrane protection for cryobiological applications.
Keywords: Ice-binding proteins, Short peptide, Self-assembly, Ice recrystallization inhibition, Cryopreservation
Keywords: Ice-binding proteins, Short peptide, Self-assembly, Ice recrystallization inhibition, Cryopreservation
