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Here, we show that a defined HS hexasaccharide, heparin\u2010dp6, efficiently inhibits RBD\u2010ACE2 binding and exhibits superior antiviral activity compared with longer HS mimetics. Electronic\u2010structure analyses suggest that the strong recognition capacity of HS arises from sulfate and carboxylate groups, which create highly negative electrostatic surfaces and serve as dominant hydrogen\u2010bond acceptors, governing charge distribution and electronic properties along the glycan backbone to modulate binding specificity and affinity. Stepwise virtual screening of a comprehensive HS database further identified several high\u2010affinity oligosaccharides, with top candidates displaying favorable RBD\u2010binding properties. These findings indicate that HS activity is determined not only by chain length and sulfation pattern, but also by the spatial arrangement of charged functional groups, providing mechanistic insight into HS\u2010RBD recognition and guiding the rational design of HS\u2010based decoy inhibitors against SARS\u2010CoV\u20102 entry.<\/jats:p>","DOI":"10.1002\/cbic.70567","type":"journal-article","created":{"date-parts":[[2026,10,10]],"date-time":"2026-10-10T06:37:11Z","timestamp":1791614231000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Heparan Sulfate Oligosaccharides Modulate SARS\u2010CoV\u20102 Spike\u2010Host Recognition"],"prefix":"10.1002","volume":"27","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-4058-180X","authenticated-orcid":false,"given":"Binjie","family":"Li","sequence":"first","affiliation":[{"name":"Beijing Advanced Innovation Center for Soft Matter Science and Engineering Beijing University 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