<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Naraga AMB</submitter><funding>Department of Science and Technology</funding><pagination>36579-36583</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9088864</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>8(64)</volume><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.</pubmed_abstract><journal>RSC advances</journal><pubmed_title>Total synthesis of μ-conotoxin lt5d.</pubmed_title><pmcid>PMC9088864</pmcid><funding_grant_id>FP140015</funding_grant_id><pubmed_authors>Naraga AMB</pubmed_authors><pubmed_authors>Villaraza AJL</pubmed_authors><pubmed_authors>Belleza OJV</pubmed_authors></additional><is_claimable>false</is_claimable><name>Total synthesis of μ-conotoxin lt5d.</name><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.</description><dates><release>2018-01-01T00:00:00Z</release><publication>2018 Oct</publication><modification>2026-05-30T20:54:44.849Z</modification><creation>2025-04-04T10:02:09.266Z</creation></dates><accession>S-EPMC9088864</accession><cross_references><pubmed>35558937</pubmed><doi>10.1039/c8ra03706j</doi></cross_references></HashMap>