Lindgren N Johan V, Varedian Miranda, Gogoll Adolf
Department of Biochemistry and Organic Chemistry, Uppsala University, Box 576, 751 23 Uppsala, Sweden.
Chemistry. 2009;15(2):501-5. doi: 10.1002/chem.200801808.
A stilbene chromophore has been incorporated into the turn region of a 42 amino acid peptide, linking two helical peptide sections. Spatial proximity between these sections, as well as aggregation into dimers, is required to facilitate the catalytic function of this artificial hydrolase. Photomodulation of the hydrolase activity results in an increase of the activity of 42 % upon switching from the trans to the cis isomer of the chromophore. This is rationalized by a change in the aggregation state of the peptidomimetic, which is supported by diffusion coefficients obtained from PFG-NMR experiments. The results show that incorporation of a small, relatively flexible chromophore into a large peptide is capable of inducing a considerable change in tertiary structure and thus, functionality.
一种芪发色团已被引入到一个42个氨基酸的肽的转角区域，连接两个螺旋肽段。这些肽段之间的空间接近度以及聚合成二聚体，对于促进这种人工水解酶的催化功能是必需的。水解酶活性的光调制导致发色团从反式异构体转变为顺式异构体时活性增加42%。这可以通过拟肽聚集状态的变化来解释，这得到了从脉冲场梯度核磁共振（PFG-NMR）实验获得的扩散系数的支持。结果表明，将一个小的、相对灵活的发色团引入到大肽中能够诱导三级结构发生相当大的变化，从而改变其功能。
