Expanding the molecular recognition repertoire of antifreeze polypeptides: effects on nucleoside crystal growth

Sen Wang, Xin Wen, Pavle Nikolovski, Vonny Juwita, Josh Fnu Arifin
  • Chemical Communications, January 2012, Royal Society of Chemistry
  • DOI: 10.1039/c2cc36264c

Beyond the ice-binding: antifreeze proteins control nucleoside crystal growth

What is it about?

Antifreeze proteins (AFPs) are often called ice-binding proteins and are thought to bind to ice or ice-like crystals exclusively to control their growth. Here molecular recognition repertoire of AFPs has been greatly expanded to other hydroxyl containing, non-ice like compounds. The inhibitory and habit-modifying effects of AFPs on the stable nuclei formation and on the crystals of nucleosides have been first demonstrated.

Why is it important?

The crystal recognition repertoire of antifreeze proteins (AFPs) has been first expanded beyond ice and ice-like crystals and the effects of AFPs on the non-ice like crystal growth are highly efficient, compared with those of other additives on crystal growth control. The finding greatly facilitates the use of AFPs in a wider range of industrial fields, such as pharmaceutical development, materials, and foods.

The following have contributed to this page: Xin Wen

Authors