{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T13:00:18Z","timestamp":1790600418293,"version":"4.1.0"},"reference-count":24,"publisher":"American Chemical Society (ACS)","issue":"9","license":[{"start":{"date-parts":[[2026,9,8]],"date-time":"2026-09-08T00:00:00Z","timestamp":1788825600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["22477049"],"award-info":[{"award-number":["22477049"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["22567020"],"award-info":[{"award-number":["22567020"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["U22A20451"],"award-info":[{"award-number":["U22A20451"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,9,28]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Protecting-group (PG)-free S-glycosylation offers an attractive strategy for glycopeptide synthesis, yet practical methods for complex peptides remain limited. Here, we report a non-photochemical S-glycosylation strategy that directly couples unprotected glycosyl donors with unprotected cysteine-containing peptides, enabling efficient access to \u03b2-S-glycopeptides. The method shows broad compatibility with glycosyl donors and peptide substrates and enables direct glycosylation of a structurally complex 37-mer precursor bearing one free cysteine, four protected cysteines, and oxidation-sensitive functionalities, thereby facilitating the efficient synthesis of sublancin and diverse glycosylated analogues. In contrast to photochemical radical-based S-glycosylation, which produces \u03b1-S-glycopeptides and proved unsuitable for the full-length substrate, the present strategy allows efficient late-stage glycosylation of structurally complex peptides. Combined with a fragment-based native chemical ligation approach for \u03b1-S-glycoside synthesis, this platform provides stereochemically defined sublancin analogues and reveals that the configuration of the S-glycosidic linkage strongly influences antibacterial activity. These results establish a practical PG-free platform for complex S-glycopeptide synthesis and glycocin structure\u2013activity studies.<\/jats:p>","DOI":"10.1021\/jacsau.6c01193","type":"journal-article","created":{"date-parts":[[2026,9,8]],"date-time":"2026-09-08T12:01:46Z","timestamp":1788868906000},"page":"5433-5438","source":"Crossref","is-referenced-by-count":0,"title":["A Protecting-Group-Free\nS-Glycosylation Strategy\nfor Complex S-Glycopeptide Synthesis"],"prefix":"10.1021","volume":"6","author":[{"given":"Ge","family":"Gao","sequence":"first","affiliation":[{"name":"Jiangxi Normal University , , 99 Ziyang Avenue , ,","place":["Nanchang, China, 330022"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jinsheng","family":"Lai","sequence":"additional","affiliation":[{"name":"Jiangxi Normal University , , 99 Ziyang Avenue , ,","place":["Nanchang, China, 330022"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jiale","family":"Chen","sequence":"additional","affiliation":[{"name":"Jiangxi Normal University , , 99 Ziyang Avenue , ,","place":["Nanchang, China, 330022"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yutian","family":"Wang","sequence":"additional","affiliation":[{"name":"Jiangxi Normal University , , 99 Ziyang Avenue , ,","place":["Nanchang, China, 330022"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6225-4183","authenticated-orcid":true,"given":"Qingju","family":"Zhang","sequence":"additional","affiliation":[{"name":"Jiangxi Normal University , , 99 Ziyang Avenue , ,","place":["Nanchang, China, 330022"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8135-2221","authenticated-orcid":true,"given":"Qi","family":"Zhang","sequence":"additional","affiliation":[{"name":"Jiangxi Normal University , , 99 Ziyang Avenue , ,","place":["Nanchang, China, 330022"]},{"name":"Fudan University , , No. 2005 Songhu Road , ,","place":["Shanghai, China, 200433"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,9,8]]},"reference":[{"issue":"5512","key":"2026092808092004900_cit1","doi-asserted-by":"publisher","first-page":"2357","DOI":"10.1126\/science.1059820","article-title":"Chemical glycobiology","volume":"291","author":"Bertozzi","year":"2001","journal-title":"Science"},{"issue":"1","key":"2026092808092004900_cit2","doi-asserted-by":"publisher","first-page":"3","DOI":"10.1093\/glycob\/cww086","article-title":"Biological\nroles of glycans","volume":"27","author":"Varki","year":"2017","journal-title":"Glycobiology"},{"issue":"27","key":"2026092808092004900_cit3","doi-asserted-by":"publisher","first-page":"3507","DOI":"10.1021\/acs.biochem.7b00268","article-title":"The Sulfur-Linked\nAnalogue of O-GlcNAc (S-GlcNAc) Is an Enzymatically Stable and Reasonable\nStructural Surrogate for O-GlcNAc at the Peptide and Protein Levels","volume":"56","author":"De Leon","year":"2017","journal-title":"Biochemistry"},{"issue":"9","key":"2026092808092004900_cit4","doi-asserted-by":"publisher","first-page":"4063","DOI":"10.1021\/jacs.8b13503","article-title":"Structure-Based Design\nof Potent Tumor-Associated Antigens: Modulation of Peptide Presentation\nby Single-Atom O\/S or O\/Se Substitutions at the Glycosidic Linkage","volume":"141","author":"Companon","year":"2019","journal-title":"J. Am. Chem. Soc."},{"issue":"1","key":"2026092808092004900_cit5","doi-asserted-by":"publisher","first-page":"108","DOI":"10.1039\/C2NP20085F","article-title":"Ribosomally\nsynthesized\nand post-translationally modified peptide natural products: overview\nand recommendations for a universal nomenclature","volume":"30","author":"Arnison","year":"2013","journal-title":"Nat. Prod. Rep."},{"issue":"1","key":"2026092808092004900_cit6","doi-asserted-by":"publisher","first-page":"130","DOI":"10.1039\/D0NP00027B","article-title":"New developments in RiPP discovery, enzymology and\nengineering","volume":"38","author":"Montalban-Lopez","year":"2021","journal-title":"Nat. Prod. Rep."},{"key":"2026092808092004900_cit7","doi-asserted-by":"publisher","first-page":"108415","DOI":"10.1016\/j.biotechadv.2024.108415","article-title":"GLYCOCINS: The sugar\npeppered antimicrobials","volume":"75","author":"Ahlawat","year":"2024","journal-title":"Biotechnol. 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