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In P1, intrachain hydrogen bonding directs the formation of a pleated structure that hierarchically assembles into hollow capsules. A glucose oxidase\u2013peroxidase assay confirmed that this unique assembly of P1 allows displaying \u223c50% glucose moieties on the outer surface, which significantly outperforms amphiphilic block copolymers. This renders outstanding multivalent binding with the lectin concanavalin A, as is evident by a very high association constant (\u223c105 M\u20131) and spontaneous glycocluster effect. In contrast, P2 or P3 fails to exhibit any notable glycocluster effect under identical conditions. Furthermore, P1, unlike P2 or P3, induced clustering of Staphylococcus aureus by targeting bacterial carbohydrate transporters, deactivated the bacteria, and prevented internalization into mammalian cells.<\/jats:p>","DOI":"10.1021\/acs.biomac.6c01170","type":"journal-article","created":{"date-parts":[[2026,8,12]],"date-time":"2026-08-12T13:02:33Z","timestamp":1786539753000},"page":"6156-6164","source":"Crossref","is-referenced-by-count":0,"title":["Chain-Folding-Regulated Assembly of an Amphiphilic\nGlycopolymer with Outstanding Functional Group Display and Multivalent\nInteractions with Biological Targets"],"prefix":"10.1021","volume":"27","author":[{"given":"Soumya","family":"Koner","sequence":"first","affiliation":[{"name":"Indian Association for the Cultivation of Science , , 2A and 2B Raja S. C. 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