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K33位乙酰化修饰SUMO蛋白的化学合成 被引量:1

Chemical Synthesis of K33 Acetylated SUMO Protein
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摘要 采用高温辅助固相合成技术及基于多肽酰肼的自然化学连接技术,高效获得了小泛素相关修饰物(SUMO)蛋白及33位赖氨酸(K33)乙酰化SUMO蛋白.聚丙烯酰胺凝胶电泳(SDS-PAGE)和圆二色光谱分析结果表明,与生物表达蛋白相比,化学合成蛋白具有较好的纯度和类似的二级结构. Sumoylated protein was found to reduce the protein binding force with the SUMO-interaction motif( SIM) of effector protein when K33 of SUMO was acetylated. To further study the structures and mechanism,a large amount of uniformity acetylated SUMO protein was greatly needed. In this work,SUMO protein and K33 acetylated SUMO protein was efficiently obtained using high temperature assisted solid-phase peptide synthesis( SPPS) technology combined with peptide hydrazide ligation. SUMO and K33 acetylated SUMO was identified with corrected molecular weight by the SDS-PAGE. It was also confirmed that the chemically synthe-tic protein and biologically expressed SUMO2 own similar homogeneity and secondary structure by the CD analysis. These results provided a foundation for the follow-up study of K33 acetylated SUMO protein.
作者 王业海 孔一夫 陈晨晨 李宜明 WANG Yehai KONG Yifu CHEN Chenchen LI Yiming(School of Biological and Medical Engineering, Hefei University of Technology, Hefei 230009, China High Magnetic Field Laboratory of the Chinese Academy of Sciences, Hefei 230031, China)
出处 《高等学校化学学报》 SCIE EI CAS CSCD 北大核心 2016年第11期1987-1992,共6页 Chemical Journal of Chinese Universities
基金 国家自然科学基金(批准号:21372058 21572043)资助~~
关键词 小泛素相关修饰物 乙酰化 高温辅助固相合成 多肽酰肼 自然化学连接 Small ubquitin-related modifier Acetylation High temperature assisted solid-phase peptide synthesis Peptide hydrazide Native chemical ligation
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参考文献40

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