检索规则说明:AND代表“并且”;OR代表“或者”;NOT代表“不包含”;(注意必须大写,运算符两边需空一格)
检 索 范 例 :范例一: (K=图书馆学 OR K=情报学) AND A=范并思 范例二:J=计算机应用与软件 AND (U=C++ OR U=Basic) NOT M=Visual
作 者:卢艳飞[1,2] 孙振刚[1] 姜莹[2] 刘巨涛[2]
机构地区:[1]辽宁师范大学化学化工学院,辽宁大连116029 [2]大连民族学院生物化学工程国家民委-教育部重点实验室,辽宁大连116605
出 处:《东北师大学报(自然科学版)》2013年第2期101-106,共6页Journal of Northeast Normal University(Natural Science Edition)
基 金:国家自然科学基金资助项目(20872013)
摘 要:以六氯环三磷腈为原料,分别与甘氨酸钠等系列支化反应,得到了3种环三磷腈甘氨酸钠支化衍生物.利用红外光谱、核磁共振波谱对化合物的结构进行了表征,详细解析了光谱数据,证实为目标产物.利用紫外-可见光谱、SDS-AGE电泳技术分别考察了衍生物对信号分子激活剂-磷酸吡哆醛、Cu2+的识别性能及与小牛血清蛋白的相互作用关系.结果表明:支化衍生物对信号分子激活剂-磷酸吡哆醛及金属Cu2+均具有明显的识别功能;支化衍生物与人体内的蛋白质及生物大分子等有较强的结合能力.Cyclotriphosphazene and its derivatives are a kind of compounds with unique structure,they can exhibit active properties in chemistry and biology,and have great research prospects in the future.Three cyclotriphosphazene glycine sodium branched derivatives were obtained from the branched reaction of hexachlorocyclotriphosphazene as original material with glycine sodium,respectively.The compounds have been characterized by IR,1H NMR,13C NMR and elemental analysis.The spectral data were interpreted in detail,all dates showed that these compounds confirmed as our target products.Besides,the recognition properties of cyclotriphosphazene derivatives with Cu2+ and signal molecule activator,namely,pyridoxal phosphate,and the interaction between derivatives and bovein serum albulim have been studied by the methods of UV-vis,SDS-agarose gel electrophoresis respectively.The results indicated that glycine branched derivatives both have obvious recognition function with pyridoxal phosphate signal molecule activator and metal Cu2+ ions.Results from the interaction with bovine serum albumin showed that glycine branched derivatives are expected to act as a kind of active drug molecules to bond with protein in the human body and biomacromolecules,this may provide an important theoretical basis for the development of new drugs.
正在载入数据...
正在载入数据...
正在载入数据...
正在载入数据...
正在载入数据...
正在载入数据...
正在载入数据...
正在链接到云南高校图书馆文献保障联盟下载...
云南高校图书馆联盟文献共享服务平台 版权所有©
您的IP:216.73.216.249