M. Aizawa, K. Yun, T. Haruyama, Y. Yanagida, E. Kobatake
{"title":"定向自组装抗体分子的蛋白质工程","authors":"M. Aizawa, K. Yun, T. Haruyama, Y. Yanagida, E. Kobatake","doi":"10.1016/S0968-5677(98)00120-5","DOIUrl":null,"url":null,"abstract":"<div><p>Two types of protein engineering have been developed for self-assembling antibody (IgG) molecules in an oriented manner. The first is to tag a cysteine group to Protein A which has a specific affinity to the Fc part of IgG. The cysteine-tagged Protein A was self-assembled on the gold surface, which was followed by self-assembling of IgG to face the antigen recognition sites to the solution phase. The second is concerned with tailing a single chain antibody by lipid at the one terminal and the hexahistidinyl group at the other. The lipid and histidine-tailed single chain antibody was embedded in a liposome to make the antigen recognition site appear on the outsphere, which was immobilized on the Ni-treated mica surface through chelating of the histidine tail. The individual liposome was clearly imaged by a tapping mode of AFM.</p></div>","PeriodicalId":22050,"journal":{"name":"Supramolecular Science","volume":"5 5","pages":"Pages 761-764"},"PeriodicalIF":0.0000,"publicationDate":"1998-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0968-5677(98)00120-5","citationCount":"4","resultStr":"{\"title\":\"Protein engineering for self-assembling antibody molecules in an oriented manner\",\"authors\":\"M. Aizawa, K. Yun, T. Haruyama, Y. Yanagida, E. Kobatake\",\"doi\":\"10.1016/S0968-5677(98)00120-5\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Two types of protein engineering have been developed for self-assembling antibody (IgG) molecules in an oriented manner. The first is to tag a cysteine group to Protein A which has a specific affinity to the Fc part of IgG. The cysteine-tagged Protein A was self-assembled on the gold surface, which was followed by self-assembling of IgG to face the antigen recognition sites to the solution phase. The second is concerned with tailing a single chain antibody by lipid at the one terminal and the hexahistidinyl group at the other. The lipid and histidine-tailed single chain antibody was embedded in a liposome to make the antigen recognition site appear on the outsphere, which was immobilized on the Ni-treated mica surface through chelating of the histidine tail. The individual liposome was clearly imaged by a tapping mode of AFM.</p></div>\",\"PeriodicalId\":22050,\"journal\":{\"name\":\"Supramolecular Science\",\"volume\":\"5 5\",\"pages\":\"Pages 761-764\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1998-10-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/S0968-5677(98)00120-5\",\"citationCount\":\"4\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Supramolecular Science\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0968567798001205\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Supramolecular Science","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0968567798001205","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Protein engineering for self-assembling antibody molecules in an oriented manner
Two types of protein engineering have been developed for self-assembling antibody (IgG) molecules in an oriented manner. The first is to tag a cysteine group to Protein A which has a specific affinity to the Fc part of IgG. The cysteine-tagged Protein A was self-assembled on the gold surface, which was followed by self-assembling of IgG to face the antigen recognition sites to the solution phase. The second is concerned with tailing a single chain antibody by lipid at the one terminal and the hexahistidinyl group at the other. The lipid and histidine-tailed single chain antibody was embedded in a liposome to make the antigen recognition site appear on the outsphere, which was immobilized on the Ni-treated mica surface through chelating of the histidine tail. The individual liposome was clearly imaged by a tapping mode of AFM.