1D Self-Assembly and Ice Recrystallization Inhibition Activity of Antifreeze Glycopeptide-Functionalized Perylene Bisimides

Chemistry. 2018 Jun 4;24(31):7834-7839. doi: 10.1002/chem.201800857. Epub 2018 May 8.

Abstract

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.

Keywords: 1D self-assembly; antifreeze glycopeptides; perylene bisimides; pi interactions; soft matter.

MeSH terms

  • Antifreeze Proteins / chemistry*
  • Crystallization
  • Glycopeptides / chemistry*
  • Ice*
  • Imides / chemistry*
  • Perylene / analogs & derivatives*
  • Perylene / chemistry
  • Protein Multimerization
  • Thermodynamics
  • Water / chemistry*

Substances

  • Antifreeze Proteins
  • Glycopeptides
  • Ice
  • Imides
  • perylene bisimide
  • Water
  • Perylene