Antifreeze Proteins (AFPs) refers to a class of polypeptides that allow cold-adapted organisms, such as fish and insects, to survive in subzero environments, by lowering the freezing point of water without affecting the melting point. This project focuses on finding the binding modes of AFPs, particularly of DAFP-1 an AFP from the beetle Dendroides canadensis, with trehalose. The binding process of this system can give a better understanding of the physiological process on how theses organisms can survive at temperatures below zero. It has been experimentally observed that a trehalose dihydrate crystal has a more favorable crystal growth rate on the (-110) plane and a least favorable rate on the (0-11) planeand it has been demonstrated that trehalose dihydrate freezing point changes drastically in the presence of DAFP-1. Using bio software programs and molecular dynamics simulation we compare and contrast the interaction between DAFP-1 with (-110) and (0-11) planes of the trehalose dehydrate crystal. It is of great interests to reveal the details of how do AFPs recognize the ligands and control the crystal growth of the substances. In addition, AFP binding conformations may yield a better understanding of the function of these remarkable proteins. Crystal growth control is essential in many scientific fields including chemistry, materials science, and pharmaceutical development. These recent findings greatly expanded the molecular recognition repertoire of AFPs, from ice-like crystals to non-ice like crystals.

Probing the binding of antifreeze proteins to trehalose crystals

248th National Meeting (2014)

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