{"title":"破解甜味药物的多样性","authors":"Sharon Yehuda, Vered Padler-Karavani","doi":"10.1038/s41589-024-01755-6","DOIUrl":null,"url":null,"abstract":"Characterization of the heterogeneity in the glycosylation of biotherapeutics is crucial for drug development but challenging. Now, an approach allows the rapid analysis of the glycosylation of intact glycoproteins, without prior processing or separation, enabling the study of glycan composition and quality assessment of any glycoprotein drug.","PeriodicalId":18832,"journal":{"name":"Nature chemical biology","volume":"20 11","pages":"1397-1398"},"PeriodicalIF":12.9000,"publicationDate":"2024-10-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Cracking the diversity of sweet drugs\",\"authors\":\"Sharon Yehuda, Vered Padler-Karavani\",\"doi\":\"10.1038/s41589-024-01755-6\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Characterization of the heterogeneity in the glycosylation of biotherapeutics is crucial for drug development but challenging. Now, an approach allows the rapid analysis of the glycosylation of intact glycoproteins, without prior processing or separation, enabling the study of glycan composition and quality assessment of any glycoprotein drug.\",\"PeriodicalId\":18832,\"journal\":{\"name\":\"Nature chemical biology\",\"volume\":\"20 11\",\"pages\":\"1397-1398\"},\"PeriodicalIF\":12.9000,\"publicationDate\":\"2024-10-24\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Nature chemical biology\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://www.nature.com/articles/s41589-024-01755-6\",\"RegionNum\":1,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Nature chemical biology","FirstCategoryId":"99","ListUrlMain":"https://www.nature.com/articles/s41589-024-01755-6","RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
Characterization of the heterogeneity in the glycosylation of biotherapeutics is crucial for drug development but challenging. Now, an approach allows the rapid analysis of the glycosylation of intact glycoproteins, without prior processing or separation, enabling the study of glycan composition and quality assessment of any glycoprotein drug.
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Nature Chemical Biology stands as an esteemed international monthly journal, offering a prominent platform for the chemical biology community to showcase top-tier original research and commentary. Operating at the crossroads of chemistry, biology, and related disciplines, chemical biology utilizes scientific ideas and approaches to comprehend and manipulate biological systems with molecular precision.
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