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首页> 外文期刊>Chembiochem: A European journal of chemical biology >Synthesis of Lysozyme-Metallacarborane Conjugates and the Effect of Boron Cluster Modification on Protein Structure and Function
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Synthesis of Lysozyme-Metallacarborane Conjugates and the Effect of Boron Cluster Modification on Protein Structure and Function

机译:溶菌酶-金属碳硼烷共轭物的合成及硼簇修饰对蛋白质结构和功能的影响

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摘要

Two complementary methods, "in solution" and "in solid state", for the synthesis of lysozyme modified with metallacarborane (cobalt bis(dicarbollide), Co(C2B9H11)(2)(2-)) were developed. As metallacarborane donors, oxonium adducts of cobalt bis(dicarbollide) and 1,4-dioxane or tetrahydropyran were used. The physicochemical and biochemical properties of the obtained lysozyme-metallacarborane conjugates were studied for changes in secondary and tertiary structure, aggregation behavior, and biological activity. Only minor changes in primary, secondary, and tertiary protein structure were observed, caused by the single substitution of metallacarborane on lysozyme. However, the modification produced significant changes in lysozyme enzymatic activity and a tendency toward time- and temperature-dependent aggregation.
机译:开发了两种互补的方法,“在溶液中”和“在固态”,用于合成用金属碳硼烷改性的溶菌酶(双(双咔唑钴),Co(C2B9H11)(2)(2-))。作为金属双碳硼烷的给体,使用了双(二咔唑钴)和1,4-二恶烷或四氢吡喃的氧鎓加合物。研究了获得的溶菌酶-金属碳硼烷共轭物的理化和生化特性,以了解其二级和三级结构,聚集行为和生物活性的变化。仅观察到一级,二级和三级蛋白质结构的微小变化,这是由金属碳碳烷在溶菌酶上的单取代所引起的。但是,该修饰在溶菌酶的酶活性上产生了显着变化,并产生了依赖于时间和温度的聚集趋势。

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