Activity of short segments of type I antifreeze protein

被引:30
|
作者
Kun, Hagit [1 ]
Mastai, Yitzhak [1 ]
机构
[1] Bar Ilan Univ, Dept Chem, IL-52900 Ramat Gan, Israel
关键词
antifreeze polypeptide; ice/water interfaces; ice growth inhibition; crystallization; WINTER FLOUNDER ANTIFREEZE; ICE GROWTH-INHIBITION; PSEUDOPLEURONECTES-AMERICANUS; SEA RAVEN; HEMITRIPTERUS-AMERICANUS; POLYPEPTIDE; FISH; BINDING; SCULPIN; GLYCOPEPTIDE-8;
D O I
10.1002/bip.20844
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In this work, we present a study on the antifreeze activity of short segments of a Type I antifreeze protein, instead of the whole protein. This approach simplifies the correlation between antifreeze protein characteristics, such as hydrophilicity/hydrophobicity, and the effect of these characteristics on the antifreeze mechanism. Three short polypeptides of Type I AFP have been synthesized. Their antifreeze activity and interactions with water and ice crystals have been analyzed by various techniques such as circular dichroism spectroscopy, X-ray diffraction, differential scanning calorimetry, and osmometry. It is shown that one short segment of Type 1 AFP has an antifreeze activity of about 60% of the native protein activity. In this work, we demonstrate that short segments of Type I AFPs possess nonzero thermal hysteresis and result in modifications in the growth habits and growth rates of ice. This approach enables the preparation of large quantities of short AFP segments at low cost with high antifreeze activity, and opens the possibility of developing the commercial potential of AFPs. (c) 2007 Wiley Periodicals, Inc.
引用
收藏
页码:807 / 814
页数:8
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