{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Stancanelli E"],"funding":["Eshelman Institute for Innovation, University of North Carolina","NHLBI NIH HHS","National Institutes of Health","National Science Foundation"],"pagination":["1207-1214"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9294993"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["17(5)"],"pubmed_abstract":["Heparan sulfate (HS) and chondroitin sulfate (CS) are two structurally distinct natural polysaccharides. Here, we report the synthesis of a library of seven structurally homogeneous HS and CS chimeric dodecasaccharides (12-mers). The synthesis was accomplished using six HS biosynthetic enzymes and four CS biosynthetic enzymes. The chimeras contain a CS domain on the reducing end and a HS domain on the nonreducing end. The synthesized chimeras display anticoagulant activity as measured by both in vitro and ex vivo experiments. Furthermore, the anticoagulant activity of <b>H/C 12-mer 5</b> is reversible by protamine, a U.S. Food and Drug Administration-approved polypeptide to neutralize anticoagulant drug heparin. Our findings demonstrate the synthesis of unnatural HS-CS chimeric oligosaccha"],"journal":["ACS chemical biology"],"pubmed_title":["Chemoenzymatic Synthesis of Homogeneous Heparan Sulfate and Chondroitin Sulfate Chimeras."],"pmcid":["PMC9294993"],"funding_grant_id":["R01 HL158932","R01 HL094463","HL144970","GM134738","R01 HL144970","HL094463","HL158932","GM123792","DMR-1933525"],"pubmed_authors":["Liu J","Li J","Arnold K","Padmanabhan A","Pham TQ","Su G","Stancanelli E","Liu W","Wander R","Pagadala V","Wang Z","Kanack A","Xu Y"],"additional_accession":[]},"is_claimable":false,"name":"Chemoenzymatic Synthesis of Homogeneous Heparan Sulfate and Chondroitin Sulfate Chimeras.","description":"Heparan sulfate (HS) and chondroitin sulfate (CS) are two structurally distinct natural polysaccharides. Here, we report the synthesis of a library of seven structurally homogeneous HS and CS chimeric dodecasaccharides (12-mers). The synthesis was accomplished using six HS biosynthetic enzymes and four CS biosynthetic enzymes. The chimeras contain a CS domain on the reducing end and a HS domain on the nonreducing end. The synthesized chimeras display anticoagulant activity as measured by both in vitro and ex vivo experiments. Furthermore, the anticoagulant activity of <b>H/C 12-mer 5</b> is reversible by protamine, a U.S. Food and Drug Administration-approved polypeptide to neutralize anticoagulant drug heparin. Our findings demonstrate the synthesis of unnatural HS-CS chimeric oligosaccha","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 May","modification":"2025-04-25T23:27:05.638Z","creation":"2025-04-06T09:21:14.082Z"},"accession":"S-EPMC9294993","cross_references":{"pubmed":["35420777"],"doi":["10.1021/acschembio.2c00146"]}}