{"title":"侧链的另一面","authors":"Fa-Jie Chen","doi":"10.1038/s41570-024-00609-y","DOIUrl":null,"url":null,"abstract":"Peptide stapling has traditionally relied on the incorporation of unnatural amino acids and symmetric stapling. A recent article targets a typically inert C–H bond within the serine side chain, offering new avenues for conformational control and side chain engineering.","PeriodicalId":18849,"journal":{"name":"Nature reviews. Chemistry","volume":"8 6","pages":"406-407"},"PeriodicalIF":38.1000,"publicationDate":"2024-05-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Another side of side chains\",\"authors\":\"Fa-Jie Chen\",\"doi\":\"10.1038/s41570-024-00609-y\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Peptide stapling has traditionally relied on the incorporation of unnatural amino acids and symmetric stapling. A recent article targets a typically inert C–H bond within the serine side chain, offering new avenues for conformational control and side chain engineering.\",\"PeriodicalId\":18849,\"journal\":{\"name\":\"Nature reviews. Chemistry\",\"volume\":\"8 6\",\"pages\":\"406-407\"},\"PeriodicalIF\":38.1000,\"publicationDate\":\"2024-05-02\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Nature reviews. Chemistry\",\"FirstCategoryId\":\"92\",\"ListUrlMain\":\"https://www.nature.com/articles/s41570-024-00609-y\",\"RegionNum\":1,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"CHEMISTRY, MULTIDISCIPLINARY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Nature reviews. Chemistry","FirstCategoryId":"92","ListUrlMain":"https://www.nature.com/articles/s41570-024-00609-y","RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, MULTIDISCIPLINARY","Score":null,"Total":0}
Peptide stapling has traditionally relied on the incorporation of unnatural amino acids and symmetric stapling. A recent article targets a typically inert C–H bond within the serine side chain, offering new avenues for conformational control and side chain engineering.
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Nature Reviews Chemistry is an online-only journal that publishes Reviews, Perspectives, and Comments on various disciplines within chemistry. The Reviews aim to offer balanced and objective analyses of selected topics, providing clear descriptions of relevant scientific literature. The content is designed to be accessible to recent graduates in any chemistry-related discipline while also offering insights for principal investigators and industry-based research scientists. Additionally, Reviews should provide the authors' perspectives on future directions and opinions regarding the major challenges faced by researchers in the field.
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