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Minimalistic ice recrystallisation inhibitors based on phenylalanine.

Matthew T WarrenIain GalpinMuhammad HasanSteven A HindmarshJohn D PadrnosCharlotte Jennifer Chante Edwards-GayleRobert T MathersDave J AdamsGabriele Cesare SossoMatthew I Gibson
Published in: Chemical communications (Cambridge, England) (2022)
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.
Keyphrases
  • small molecule
  • signaling pathway
  • soft tissue
  • tandem mass spectrometry