{"id":{"repo_id":"slu","oai_identifier":"oai:pub.epsilon.slu.se:194"},"canonical_url":"https://search.dev.ndltd.org/etd/slu/oai:pub.epsilon.slu.se:194","repository":{"repo_id":"slu","name":"Swedish University of Agricultural Sciences","base_url":"https://pub.epsilon.slu.se/cgi/oai2"},"display":{"title":"Structural studies of saccharides and glycopeptides in aqueous solution by 1H NMR spectroscopy","abstract":"The first part of this thesis describes the use of hydroxy protons for 1H NMR conformational studies of saccharides and small glycopeptide performed in aqueous solution. The conformations of the disaccharide b-D-GlcpNAc-(1®4)-b-D-GlcNAc and of the glycoside b-D-Galp-(1®3)-a-D-GalpNAc-O-Me have been investigated and compared to those of the amino acid linked counterparts b-D-GlcpNAc-(1®4)-b-D-GlcNAc-N-Asn and b-D-Galp-(1®3)-a-D-GalpNAc-O-Ser. For this, the hydroxy proton chemical shifts, vicinal coupling constants, temperature coefficients, exchange rates with water and NOEs were measured. The V[b-D-Galp-(1®3)-a-D-GalpNAc-(1®]THPGY glycopeptide was also investigated. Information about hydrogen bonding interactions and hydration could be obtained. The second part of this thesis describes the 1H NMR studies of the solution conformation of the conotoxin contulakin-G and five analogues. The five analogues had different biological activities, all being less active than contulakin-G. The conformational studies were performed in an attempt to correlate the structure to the activity. Contulakin-G is a 16 amino acid O-glycosylated glycopeptide, which originally was isolated from the venom of the Cone snail Conus geographus. It has the sequence ZSEEGGSNAT*KKPYIL with the disaccharide b-D-Galp-(1®3)-a-D-GalpNAc attached to the threonine residue in position 10. It has entered phase II clinical trials for short-term management of post-operative pain. The five analogues are the non-glycosylated peptide, one glycopeptide with the monosaccharide a-D-GalpNAc attached to Thr10, one with the disaccharide attached at Ser7, and two enantiomeric analogues where the disaccharide was attached at the L-Ser10 and D-ser10 residues, respectively. The NMR studies showed that in all compounds, the peptide predominantly existed in extended conformations. Transient populations of folded conformations were found in the glycosylated peptides. The two most active compounds, contulakin-G, and the (D-Ser10) glycosylated analogue, displayed some similar conformational features.","abstract_html":"The first part of this thesis describes the use of hydroxy protons for 1H NMR conformational studies of saccharides and small glycopeptide performed in aqueous solution. The conformations of the disaccharide b-D-GlcpNAc-(1®4)-b-D-GlcNAc and of the glycoside b-D-Galp-(1®3)-a-D-GalpNAc-O-Me have been investigated and compared to those of the amino acid linked counterparts b-D-GlcpNAc-(1®4)-b-D-GlcNAc-N-Asn and b-D-Galp-(1®3)-a-D-GalpNAc-O-Ser. For this, the hydroxy proton chemical shifts, vicinal coupling constants, temperature coefficients, exchange rates with water and NOEs were measured. The V[b-D-Galp-(1®3)-a-D-GalpNAc-(1®]THPGY glycopeptide was also investigated. Information about hydrogen bonding interactions and hydration could be obtained. The second part of this thesis describes the 1H NMR studies of the solution conformation of the conotoxin contulakin-G and five analogues. The five analogues had different biological activities, all being less active than contulakin-G. The conformational studies were performed in an attempt to correlate the structure to the activity. Contulakin-G is a 16 amino acid O-glycosylated glycopeptide, which originally was isolated from the venom of the Cone snail Conus geographus. It has the sequence ZSEEGGSNAT*KKPYIL with the disaccharide b-D-Galp-(1®3)-a-D-GalpNAc attached to the threonine residue in position 10. It has entered phase II clinical trials for short-term management of post-operative pain. The five analogues are the non-glycosylated peptide, one glycopeptide with the monosaccharide a-D-GalpNAc attached to Thr10, one with the disaccharide attached at Ser7, and two enantiomeric analogues where the disaccharide was attached at the L-Ser10 and D-ser10 residues, respectively. The NMR studies showed that in all compounds, the peptide predominantly existed in extended conformations. Transient populations of folded conformations were found in the glycosylated peptides. The two most active compounds, contulakin-G, and the (D-Ser10) glycosylated analogue, displayed some similar conformational features.","abstract_has_math":false,"creators":["Lill Kindahl"],"institution":null,"degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2003,"date_issued":"2003-03","date_published":"2003-03","updated_at":"2026-07-24T04:35:38Z","subjects":["carbohydrates","peptides","solutions","hydrogen","spectrometry","hydroxy proton","contulakin-G","conotoxin","conformational analysis","hydrogen bond","O-glycosylation"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://pub.epsilon.slu.se/194/","outbound_label":"Repository record","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.issued","label":"Date","values":["2003-03"]},{"key":"dc:type","label":"Dc Type","values":["Doctoral thesis"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["carbohydrates","peptides","solutions","hydrogen","spectrometry","hydroxy proton","contulakin-G","conotoxin","conformational analysis","hydrogen bond","O-glycosylation"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["https://pub.epsilon.slu.se/194/","https://pub.epsilon.slu.se/194/1/phd_thesis_kindahl.pdf"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.other","label":"Dc Description Other","values":["The first part of this thesis describes the use of hydroxy protons for 1H NMR conformational studies of saccharides and small glycopeptide performed in aqueous solution. The conformations of the disaccharide b-D-GlcpNAc-(1®4)-b-D-GlcNAc and of the glycoside b-D-Galp-(1®3)-a-D-GalpNAc-O-Me have been investigated and compared to those of the amino acid linked counterparts b-D-GlcpNAc-(1®4)-b-D-GlcNAc-N-Asn and b-D-Galp-(1®3)-a-D-GalpNAc-O-Ser. For this, the hydroxy proton chemical shifts, vicinal coupling constants, temperature coefficients, exchange rates with water and NOEs were measured. The V[b-D-Galp-(1®3)-a-D-GalpNAc-(1®]THPGY glycopeptide was also investigated. Information about hydrogen bonding interactions and hydration could be obtained. The second part of this thesis describes the 1H NMR studies of the solution conformation of the conotoxin contulakin-G and five analogues. The five analogues had different biological activities, all being less active than contulakin-G. The conformational studies were performed in an attempt to correlate the structure to the activity. Contulakin-G is a 16 amino acid O-glycosylated glycopeptide, which originally was isolated from the venom of the Cone snail Conus geographus. It has the sequence ZSEEGGSNAT*KKPYIL with the disaccharide b-D-Galp-(1®3)-a-D-GalpNAc attached to the threonine residue in position 10. It has entered phase II clinical trials for short-term management of post-operative pain. The five analogues are the non-glycosylated peptide, one glycopeptide with the monosaccharide a-D-GalpNAc attached to Thr10, one with the disaccharide attached at Ser7, and two enantiomeric analogues where the disaccharide was attached at the L-Ser10 and D-ser10 residues, respectively. The NMR studies showed that in all compounds, the peptide predominantly existed in extended conformations. Transient populations of folded conformations were found in the glycosylated peptides. The two most active compounds, contulakin-G, and the (D-Ser10) glycosylated analogue, displayed some similar conformational features."]},{"key":"dc:title","label":"Title","values":["Structural studies of saccharides and glycopeptides in aqueous solution by 1H NMR spectroscopy","Acta Universitatis Agriculturae Sueciae. Agraria"]}]}],"canonical_facts":{"dc:date.issued":["2003-03"],"dc:description.other":["The first part of this thesis describes the use of hydroxy protons for 1H NMR conformational studies of saccharides and small glycopeptide performed in aqueous solution. The conformations of the disaccharide b-D-GlcpNAc-(1®4)-b-D-GlcNAc and of the glycoside b-D-Galp-(1®3)-a-D-GalpNAc-O-Me have been investigated and compared to those of the amino acid linked counterparts b-D-GlcpNAc-(1®4)-b-D-GlcNAc-N-Asn and b-D-Galp-(1®3)-a-D-GalpNAc-O-Ser. For this, the hydroxy proton chemical shifts, vicinal coupling constants, temperature coefficients, exchange rates with water and NOEs were measured. The V[b-D-Galp-(1®3)-a-D-GalpNAc-(1®]THPGY glycopeptide was also investigated. Information about hydrogen bonding interactions and hydration could be obtained. The second part of this thesis describes the 1H NMR studies of the solution conformation of the conotoxin contulakin-G and five analogues. The five analogues had different biological activities, all being less active than contulakin-G. The conformational studies were performed in an attempt to correlate the structure to the activity. Contulakin-G is a 16 amino acid O-glycosylated glycopeptide, which originally was isolated from the venom of the Cone snail Conus geographus. It has the sequence ZSEEGGSNAT*KKPYIL with the disaccharide b-D-Galp-(1®3)-a-D-GalpNAc attached to the threonine residue in position 10. It has entered phase II clinical trials for short-term management of post-operative pain. The five analogues are the non-glycosylated peptide, one glycopeptide with the monosaccharide a-D-GalpNAc attached to Thr10, one with the disaccharide attached at Ser7, and two enantiomeric analogues where the disaccharide was attached at the L-Ser10 and D-ser10 residues, respectively. The NMR studies showed that in all compounds, the peptide predominantly existed in extended conformations. Transient populations of folded conformations were found in the glycosylated peptides. The two most active compounds, contulakin-G, and the (D-Ser10) glycosylated analogue, displayed some similar conformational features."],"dc:identifier.uri":["https://pub.epsilon.slu.se/194/","https://pub.epsilon.slu.se/194/1/phd_thesis_kindahl.pdf"],"dc:subject":["carbohydrates","peptides","solutions","hydrogen","spectrometry","hydroxy proton","contulakin-G","conotoxin","conformational analysis","hydrogen bond","O-glycosylation"],"dc:title":["Structural studies of saccharides and glycopeptides in aqueous solution by 1H NMR spectroscopy","Acta Universitatis Agriculturae Sueciae. Agraria"],"dc:type":["Doctoral thesis"]},"updated_at":"2026-07-24T04:35:38Z"}