Article(id=1242133864131408031, tenantId=1146029695717560320, journalId=1146031591421210625, issueId=1242133836251869266, articleNumber=null, orderNo=16, doi=10.3981/j.issn.1000-7857.2015.17.011, pmid=null, cstr=null, oa=null, hot=null, price=null, onlineType=0, articleFormat=0, articleType=null, articleTypeStr=null, receivedDate=1427040000000, receivedDateStr=2015-03-23, revisedDate=1434902400000, revisedDateStr=2015-06-22, acceptedDate=null, acceptedDateStr=null, onlineDate=1442036797513, onlineDateStr=2015-09-12, pubDate=1442073600000, pubDateStr=2015-09-13, doiRegisterDate=null, doiRegisterDateStr=null, onlineIssueDate=1442036797513, onlineIssueDateStr=2015-09-12, onlineJustAcceptDate=null, onlineJustAcceptDateStr=null, onlineFirstDate=null, onlineFirstDateStr=null, sourceXml=null, magXml=null, createTime=1774077390935, creator=sys-migrate, updateTime=1774077390935, updator=sys-migrate, issue=Issue{id=1242133836251869266, tenantId=1146029695717560320, journalId=1146031591421210625, year='2015', volume='33', issue='17', pageStart='1', pageEnd='112', issueExtLink='null', onlineDate='null', pubDate='1442073600000', pubDateStr='2015-09-13', beforeIssueId=null, nextIssueId=null, price=null, status=1, issueComplete=1, articleOrder=3, issueType=-1, specialIssue=null, createTime=1774077384289, creator='sys-migrate', updateTime=1774077384289, updator='sys-migrate', preIssue=null, nextIssue=null, articleTotal=null, ext=null, issueFiles=null, downloadFileDto=null}, startPage=96, endPage=101, ext={EN=ArticleExt(id=1242133867524595826, articleId=1242133864131408031, tenantId=1146029695717560320, journalId=1146031591421210625, language=EN, title=Binding interaction of carbonic anhydrase-liposome complex and medicinal molecules by Scatchard method, columnId=1242116080374710456, journalTitle=Science & Technology Review, columnName=Articles, runingTitle=null, highlight=null, articleAbstract=In this in vitro study, carbonic anhydrase-liposome complex was prepared to simulate the in vivo interactions between drug molecules and carbonic anhydrase. The complex was prepared by ultrasonic cell disruption, mixing and extrusion. Zeta potential and the size of carbonic anhydrase-liposome complex were -45.06 mV and 99.43 nm, respectively, indicating this complex is stable and suitable to apply for capillary electrophoresis. The complex was further added in running buffers as pseudo stationary phase in capillary electrophoresis, and 4-carboxybenzenesulfonamide (containing 2.2×10^-3 mol/L 4-methyl-2-pentanone as EOF marker) was added as a sample to establish the model of the interaction between the drug and carbonic anhydrase-liposome complex using Scatchard method. The binding constant in this model was 1.172×10⁴mL·g^-1. Among the 12 drugs studied using this method, caffeic acid, L-ascorbic acid, 2,4-dichloro-5-sulfamoylbenzoic acid, and 4-chloro-3-sulfamoyl benzoic acid had strong interactions with carbonic anhydrase-liposome complex, having higher binding constants than that of 4-carboxybenzenesulfonamide. Ferulic acid, aristolochic acid, gallic acid, protocatechuic acid, and nicotinic acid had weak interactions with carbonic anhydrase-liposome complex, having lower binding constants than that of 4-carboxybenzenesulfonamide. This method can be used to check interactions between carbonic anhydrase or other targets and drug molecules rapidly and effectively, reducing the development cycle of drugs., authors=HU Yinghui, DAI Rongji, AN Jing, QIAN Qingqing, DENG Yulin, authorsList=HU Yinghui, DAI Rongji, AN Jing, QIAN Qingqing, DENG Yulin, authorCompany=School of Life Science, Beijing Institute of Technology, Beijing 100081, China, correspAuthors=null, authorNote=null, correspAuthorsNote=null, copyrightStatement=null, copyrightOwner=null, extLink=null, articleAbsUrl=null, sourceXml=null, magXml=null, pdfUrl=null, pdf=4gYe8S2kxf9I6x0T6rDJ2g==, pdfFileSize=2787835, pdfExtLink=null, richHtmlUrl=null, mobilePdfUrl=null, reviewReport=null, pdfFirstPage=null, abstractGraph=null, abstractGraphContent=null, abstractVideo=null, citation=null, cebUrl=null, magXmlContent=null, mapNumber=null, fund=null), CN=ArticleExt(id=1242133866543132842, articleId=1242133864131408031, tenantId=1146029695717560320, journalId=1146031591421210625, language=CN, title=基于Scatchard法的碳酸酐酶-脂质体与药物结合常数测定, columnId=1146540929516700224, journalTitle=科技导报, columnName=研究论文, runingTitle=null, highlight=null, articleAbstract=为更好地模拟药物小分子与碳酸酐酶在体内的相互作用,采用碳酸酐酶-脂质体毛细管电泳法,以4-羧基苯磺酰胺为分析对象建立碳酸酐酶药物筛选模型,并以此模型为基础计算12 种药物小分子与碳酸酐酶的结合常数,分析药物小分子与碳酸酐酶的相互作用。结果表明,4-羧基苯磺酰胺与碳酸酐酶-脂质体的结合常数为1.172×10⁴ mL·g^-1,具有较强的相互作用。基于此,筛选出4 种(咖啡酸、L-抗坏血酸、2, 4-二氯-5-磺酰胺基苯甲酸和4-氯-3-磺酰胺基苯甲酸)和5种(阿魏酸、马兜铃酸、没食子酸、原儿茶酸、烟酸)与复合物具有较强或较弱相互作用的药物。通过该法可快速、有效、经济地测定碳酸酐酶或其他靶标与药物的相互作用,缩短药物研发周期。, authors=胡英慧, 戴荣继, 安静, 钱庆庆, 邓玉林, authorsList=胡英慧, 戴荣继, 安静, 钱庆庆, 邓玉林, authorCompany=北京理工大学生命学院, 北京100081, correspAuthors=null, authorNote=胡英慧,博士研究生,研究方向为药物筛选,电子信箱:hyhjx@bit.edu.cn, correspAuthorsNote=戴荣继,教授,研究方向为生物分子分离新材料与分析新方法、药物合成、药物快速筛选等,电子信箱:dairongji@bit.edu.cn, copyrightStatement=null, copyrightOwner=null, extLink=null, articleAbsUrl=null, sourceXml=null, magXml=null, pdfUrl=null, pdf=yVTtf4ecnHVQfT0ARDhYrA==, pdfFileSize=2787835, pdfExtLink=null, richHtmlUrl=null, 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