Dr. Daishiro Kobayashi, Dr. Masaya Denda, Junya Hayashi, Kota Hidaka, Yutaka Kohmura, Dr. Takaaki Tsunematsu, Dr. Kohei Nishino, Dr. Harunori Yoshikawa, Dr. Kento Ohkawachi, Dr. Kiyomi Nigorikawa, Dr. Tetsuro Yoshimaru, Prof. Naozumi Ishimaru, Prof. Wataru Nomura, Prof. Toyomasa Katagiri, Prof. Hidetaka Kosako, Prof. Akira Otaka
{"title":"封面专题：过氧化硫介导的 Cys-Trp 选择性生物键合可实现蛋白质标记和多肽异源二聚化（欧洲化学 3-4/2024 期）","authors":"Dr. Daishiro Kobayashi, Dr. Masaya Denda, Junya Hayashi, Kota Hidaka, Yutaka Kohmura, Dr. Takaaki Tsunematsu, Dr. Kohei Nishino, Dr. Harunori Yoshikawa, Dr. Kento Ohkawachi, Dr. Kiyomi Nigorikawa, Dr. Tetsuro Yoshimaru, Prof. Naozumi Ishimaru, Prof. Wataru Nomura, Prof. Toyomasa Katagiri, Prof. Hidetaka Kosako, Prof. Akira Otaka","doi":"10.1002/ceur.202400047","DOIUrl":null,"url":null,"abstract":"<p><b>A tryptophan modification</b> that utilizes S-acetamidomethyl cysteine sulfoxide under mildly acidic conditions with magnesium chloride was achieved. An optimum condition in an ionic liquid allowed antibody modification without significant denaturation. In their Research Article, A. Otaka and co-workers describe the difference in chemical behaviors to acids between S-acetamidomethyl and <i>p</i>-methoxybenzyl cysteine sulfoxides permitted peptide heterodimerization in a one-pot sequential manner.\n <figure>\n <div><picture>\n <source></source></picture><p></p>\n </div>\n </figure>\n </p>","PeriodicalId":100234,"journal":{"name":"ChemistryEurope","volume":"2 3-4","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2024-07-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/ceur.202400047","citationCount":"0","resultStr":"{\"title\":\"Cover Feature: Sulfoxide-Mediated Cys-Trp-Selective Bioconjugation that Enables Protein Labeling and Peptide Heterodimerization (ChemistryEurope 3-4/2024)\",\"authors\":\"Dr. Daishiro Kobayashi, Dr. Masaya Denda, Junya Hayashi, Kota Hidaka, Yutaka Kohmura, Dr. Takaaki Tsunematsu, Dr. Kohei Nishino, Dr. Harunori Yoshikawa, Dr. Kento Ohkawachi, Dr. Kiyomi Nigorikawa, Dr. Tetsuro Yoshimaru, Prof. Naozumi Ishimaru, Prof. Wataru Nomura, Prof. Toyomasa Katagiri, Prof. Hidetaka Kosako, Prof. Akira Otaka\",\"doi\":\"10.1002/ceur.202400047\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><b>A tryptophan modification</b> that utilizes S-acetamidomethyl cysteine sulfoxide under mildly acidic conditions with magnesium chloride was achieved. An optimum condition in an ionic liquid allowed antibody modification without significant denaturation. In their Research Article, A. Otaka and co-workers describe the difference in chemical behaviors to acids between S-acetamidomethyl and <i>p</i>-methoxybenzyl cysteine sulfoxides permitted peptide heterodimerization in a one-pot sequential manner.\\n <figure>\\n <div><picture>\\n <source></source></picture><p></p>\\n </div>\\n </figure>\\n </p>\",\"PeriodicalId\":100234,\"journal\":{\"name\":\"ChemistryEurope\",\"volume\":\"2 3-4\",\"pages\":\"\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2024-07-08\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://onlinelibrary.wiley.com/doi/epdf/10.1002/ceur.202400047\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"ChemistryEurope\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://onlinelibrary.wiley.com/doi/10.1002/ceur.202400047\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"ChemistryEurope","FirstCategoryId":"1085","ListUrlMain":"https://onlinelibrary.wiley.com/doi/10.1002/ceur.202400047","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Cover Feature: Sulfoxide-Mediated Cys-Trp-Selective Bioconjugation that Enables Protein Labeling and Peptide Heterodimerization (ChemistryEurope 3-4/2024)
A tryptophan modification that utilizes S-acetamidomethyl cysteine sulfoxide under mildly acidic conditions with magnesium chloride was achieved. An optimum condition in an ionic liquid allowed antibody modification without significant denaturation. In their Research Article, A. Otaka and co-workers describe the difference in chemical behaviors to acids between S-acetamidomethyl and p-methoxybenzyl cysteine sulfoxides permitted peptide heterodimerization in a one-pot sequential manner.
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