Laboratory of Chemical Biology and Bioengineering, Graduate School and Faculty of Environmental Engineering, The University of Kitakyushu, Kitakyushu 808-0135, Japan.
Med Hypotheses. 2011 Aug;77(2):159-61. doi: 10.1016/j.mehy.2011.03.008. Epub 2011 Jun 12.
Novel catalytic peptides highly active in conversion of hydrogen peroxide to superoxide are newly designed and proposed as novel probes for assessing the cellular protein phosphorylation/dephosphorylation events possibly available for future clinical applications. One of model peptide was invented by fusing the copper-binding catalytic peptide and Erk1/2 MAP kinase kinase substrate peptide. In order to demonstrate that this type of probes is phosphorylation-sensitive, preliminary data was obtained with non-phosphorylated and phosphorylated peptides at two phosphorylation sites, namely, threonine and tyrosine residues. As expected, model phosphorylations effectively lowered the catalytic activity of the peptide. This is the first implication that phosphorylation-controllable enzyme mimics could be artificially invented. In addition, the author propose a possible application of this type of peptides as the tools or components for constructing a simplified in vitro signaling system processing the phosphorylation signals into the oxidative signals possibly affecting the fate of the living cells.
新型催化肽在将过氧化氢转化为超氧阴离子方面具有很高的活性，被新设计并提出作为评估细胞蛋白质磷酸化/去磷酸化事件的新型探针，可能可用于未来的临床应用。其中一种模型肽是通过融合铜结合催化肽和 Erk1/2 MAP 激酶激酶底物肽而发明的。为了证明这种探针是磷酸化敏感的，在两个磷酸化位点，即苏氨酸和酪氨酸残基上，获得了未经磷酸化和磷酸化肽的初步数据。正如预期的那样，模型磷酸化有效地降低了肽的催化活性。这是第一个暗示可以人工发明可磷酸化控制的酶模拟物的实例。此外，作者提出了将这种肽作为构建简化的体外信号系统的工具或组件的一种可能应用，该系统将磷酸化信号转化为可能影响活细胞命运的氧化信号。
