摘要
目的运用蛋白质折叠码和分子对接技术对治疗幽门螺杆菌感染的常用抗生素的耐药性进行解释。方法通过使用蛋白质折叠码和分子对接技术对治疗幽门螺杆菌感染的多个抗生素药物靶点区结构进行了分析。结果耐药性较强的3种抗生素的靶蛋白靶点结构存在着高度保守性。敏感度较好的痢特灵的靶点结构较其他药靶有所改变。结论从抗生素结合靶位点的结构上可以很好地解释常用抗生素的耐药问题,为新型抗生素设计提供了有益的线索。
Objective To analyse Helicobacter priori (Hp) infection antibiotics resistance using of protein folding shape code and molecular docking technology. Methods The use of protein folding shape code and molecular docking technology for the treatment af Hp infection in multiple antibiotic drug target zones was analyzed. Results The target pro- tein binding site structurers of three antibiotics which were highly resistant to drugs were highly conservative. The furazoli- done target structure was changed more considerably than other drug targets. Conclusion Our results offer a good explana- tion of the resistance of several common antibiotics from the structure view.
出处
《军事医学》
CAS
CSCD
北大核心
2012年第5期381-384,共4页
Military Medical Sciences
基金
浙江省科技计划项目资助(2011C23140)
关键词
蛋白质折叠码
分子对接
抗生素
耐药性
protein folding shape code
molecular docking
antibiotic
drug resistance