Wen D, Laursen R A
Department of Chemistry, Boston University, MA 02215.
FEBS Lett. 1993 Feb 8;317(1-2):31-4. doi: 10.1016/0014-5793(93)81485-i.
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 ellipticites. 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.
已化学合成了α-螺旋抗冻多肽（AFP）的D型和L型。这些分子的圆二色光谱显示出大小相等、方向相反的椭圆率。单独的D型和L型对映体以及二者50:50的混合物均表现出相同的抗冻活性，但预计对映体形式与冰表面结合的方向不同。有人提出，某些冰表面的对称性允许AFP进行不对称结合，因此AFP类似于作用于前手性底物的酶。
