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Minimalistic ice recrystallisation inhibitors based on phenylalanine.

ABSTRACT: 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.

SUBMITTER: Warren MT

PROVIDER: S-EPMC9260883 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature

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Minimalistic ice recrystallisation inhibitors based on phenylalanine.

Warren Matthew T MT Galpin Iain I Hasan Muhammad M Hindmarsh Steven A SA Padrnos John D JD Edwards-Gayle Charlotte C Mathers Robert T RT Adams Dave J DJ Sosso Gabriele C GC Gibson Matthew I MI

Chemical communications (Cambridge, England) 20220707 55

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. So ...[more]

PMID: 35723608

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