A D-ANTIFREEZE POLYPEPTIDE DISPLAYS THE SAME ACTIVITY AS ITS NATURAL L-ENANTIOMER
A D-ANTIFREEZE POLYPEPTIDE DISPLAYS THE SAME ACTIVITY AS ITS NATURAL L-ENANTIOMER
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DOI：
10.1016/0014-5793(93)81485-i
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发表时间：
1993-02-08
期刊：
影响因子：
3.5
通讯作者：
LAURSEN, RA
中科院分区：
文献类型：
--
作者：
WEN, DY;LAURSEN, RA
本文合成了一种α -螺旋型抗冻多肽（AFP）的D型和l型。分子的圆二色光谱显示出相等和相反的椭圆度。单独的D-和l -对映体，以及两者50:50的混合物，都显示出相同的抗冻活性，但对映体形式被预测以不同的方向结合在冰面上。这表明，某些冰表面的对称性允许蛋白质的不对称结合，因此蛋白质蛋白质类似于作用于前手性底物的酶。
The D- and L-forms of an alpha-helical antifreeze polypeptide (AFP) have been chemically synthesized. Circular dichroism spectra of the molecules show equal and opposite ellipticities. The D- and the L-enantiomers alone, and a 50:50 mixture of the two, all show identical antifreeze activity, but the enantiomeric forms are predicted to bind to the ice surface with different orientations. It is suggested that symmetry properties of certain ice surfaces permit the asymmetric binding of AFPs, and thus that AFPs are analogous to enzymes that act upon prochiral substrates.