1D self-assembly and ice recrystallization inhibition activity of antifreeze glycopeptide-functionalized perylene bisimides

Madeleine K. Adam, Charles Jarrett-Wilkins, Michael Beards, Emiliyan Staykov, Liam R. MacFarlane, Toby D.M. Bell, Jacqueline M. Matthews, Ian Manners, Charl F.J. Faul, Pierre D.J. Moens, Robert N. Ben, Brendan L. Wilkinson

Research output: Contribution to journalArticleResearchpeer-review

14 Citations (Scopus)


Antifreeze glycoproteins (AFGPs) are polymeric natural products that have drawn considerable interest in diverse research fields owing to their potent ice recrystallization inhibition (IRI) activity. Self-assembled materials have emerged as a promising class of biomimetic ice growth inhibitor, yet the development of AFGP-based supramolecular materials that emulate the aggregative behavior of AFGPs have not yet been reported. This work reports the first example of the 1D self-assembly and IRI activity of AFGP-functionalized perylene bisimides (AFGP-PBIs). Glycopeptide-functionalized PBIs underwent 1D self-assembly in water and showed modest IRI activity, which could be tuned through substitution of the PBI core. This work presents essential proof-of-principle for the development of novel IRIs as potential supramolecular cryoprotectants and glycoprotein mimics.

Original languageEnglish
Pages (from-to)7834-7839
Number of pages6
JournalChemistry - A European Journal
Issue number31
Publication statusPublished - 4 Jun 2018


  • 1D self-assembly
  • antifreeze glycopeptides
  • perylene bisimides
  • pi interactions
  • soft matter

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