Minimalistic ice recrystallisation inhibitors based on phenylalanine

Ice recrystallisation inhibition (IRI) is typically associated with ice binding proteins, but polymers and other mimetics are emerging. Here we identify phenylalanine as a minimalistic, yet potent, small-molecule IRI capable of inhibiting ice growth at just 1 mg mL −1 . Facial amphiphilicity is shown to be a crucial structural feature, with para -substituents enhancing (hydrophobic) or decreasing (hydrophilic) IRI activity. Both amino and acid groups were found to be essential. Solution-phase self-assembly of Phenylalanine was not observed, but the role of self-assembly at the ice/water interface could not be ruled out as a contributing factor. Phenylalanine is demonstrated to inhibit ice recrystallisation at low mM concentrations. Sequential modifications demonstrate the importance of amphiphilicity on activity.