Gopishetty Bhaskar, Ren Lige, Waller Tiffany M, Wavreille Anne-Sophie, Lopez Miguel, Thakkar Amit, Zhu Jinge, Pei Dehua
Department of Chemistry and Ohio State Biochemistry Program, The Ohio State University, 100 West 18th Avenue, Columbus, Ohio 43210, USA.
Org Lett. 2008 Oct 16;10(20):4605-8. doi: 10.1021/ol801868a. Epub 2008 Sep 18.
Fully protected 3,5-difluorotyrosine (F2Y), Fmoc-F2Y(tBu)-OH, is efficiently prepared by a chemoenzymatic process and incorporated into individual peptides and combinatorial peptide libraries. The F2Y-containing peptides display kinetic properties toward protein tyrosine phosphatases (PTPs) similar to their corresponding tyrosine-containing counterparts but are resistant to tyrosinase action. These properties make F2Y a useful tyrosine surrogate during peptide library screening for optimal PTP substrates.
通过化学酶法高效制备了完全保护的3,5-二氟酪氨酸(F2Y),即Fmoc-F2Y(tBu)-OH,并将其掺入单个肽和组合肽库中。含F2Y的肽对蛋白质酪氨酸磷酸酶(PTP)显示出与相应含酪氨酸的对应物相似的动力学特性,但对酪氨酸酶作用具有抗性。这些特性使F2Y在筛选最佳PTP底物的肽库过程中成为一种有用的酪氨酸替代物。