完全交替的聚碳酸亚环己酯可用作微电子牺牲材料,文中用水杨醛,邻苯二胺和叔丁醇铝制备了SalenAlOC(CH3)3,以N,N-二甲胺基吡啶(DMAP)作为共催化剂催化二氧化碳和氧化环己烯共聚,用核磁共振(1H-NMR)对共聚产物进行了结构分析。结果表明,催化效率最高可达494 g Polym/g Cat,共聚产物中的碳酸酯键含量为99.9%,-Mn=30300 g/mol,分子量分布PDI=1.46;与SalenAl(OiPr)相比,SalenAlOC(CH3)3得到交替度大于99%的共聚产物的反应条件更宽,更加容易控制。
Objective The protozoan Toxoplasma gondii expresses large amounts of a 37 kDa Type 2C serine-threonine phosphatase,the so-called TgPP2 C which has been suggested to contribute to parasite growth regulation.Ectopic expression in mammalian cells also indicated that the enzyme could regulate growth and survival.In this study,we aimed to investigate the interaction of TgPP2 C with human SSRP1(structure-specific recognition protein 1) and the effects of TgPP2 C on cell viability.Methods The yeast two hybrid system,His-tag pull-down and co-immunoprecipitation assays were used to confirm the interaction of TgPP2 C with SSRP1 and determine the binding domain on SSRP1.The evaluation of cell apoptosis was performed using cleaved caspase-3 antibody and Annexin-V/PI kit combined with flow cytometry.Results We identified human SSRP1 as an interacting partner of TgPP2 C.The C-terminal region of SSRP1 including the amino acids 471 to 538 was specifically mapped as the region responsible for interaction with TgPP2 C.The overexpression of TgPP2 C down-regulated cell apoptosis and negatively regulated apoptosis induced by DRB,casein kinase II(CKII) inhibitor,through enhanced interaction with SSRP1.Conclusion TgPP2 C may be a parasitic factor capable of promoting cell survival through interaction with the host protein SSRP1,thereby creating a favorable environment for parasite growth.
GAO Xue JuanFENG Jun XiaZHU SenLIU Xiao HuiTARDIEUX IsabelleLIU Lang Xia