{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Naraga AMB"],"funding":["Department of Science and Technology"],"pagination":["36579-36583"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9088864"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["8(64)"],"pubmed_abstract":["The total synthesis of μ-conotoxin lt5d is presented for the first time employing two different strategies. One involves glutathione-assisted oxidation where all disulphide linkages are formed simultaneously. Another involves orthogonal protection of cysteine residues, allowing the controlled formation of disulphide linkages sequentially. Both methods achieve the same peptide."],"journal":["RSC advances"],"pubmed_title":["Total synthesis of μ-conotoxin lt5d."],"pmcid":["PMC9088864"],"funding_grant_id":["FP140015"],"pubmed_authors":["Naraga AMB","Villaraza AJL","Belleza OJV"],"additional_accession":[]},"is_claimable":false,"name":"Total synthesis of μ-conotoxin lt5d.","description":"The total synthesis of μ-conotoxin lt5d is presented for the first time employing two different strategies. One involves glutathione-assisted oxidation where all disulphide linkages are formed simultaneously. Another involves orthogonal protection of cysteine residues, allowing the controlled formation of disulphide linkages sequentially. Both methods achieve the same peptide.","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Oct","modification":"2026-05-30T20:54:44.849Z","creation":"2025-04-04T10:02:09.266Z"},"accession":"S-EPMC9088864","cross_references":{"pubmed":["35558937"],"doi":["10.1039/c8ra03706j"]}}