{"id":{"repo_id":"qu-belfast","oai_identifier":"oai:pure.qub.ac.uk/portal:studenttheses/aff69d08-c0ad-4108-81bd-5d6d86682fd4"},"canonical_url":"https://search.dev.ndltd.org/etd/qu-belfast/oai:pure.qub.ac.uk/portal:studenttheses/aff69d08-c0ad-4108-81bd-5d6d86682fd4","repository":{"repo_id":"qu-belfast","name":"Queen's University Belfast","base_url":"https://pureadmin.qub.ac.uk/ws/oai"},"display":{"title":"The discovery and bioactivity evaluation of a novel peptide, QUB-2652, from the skin secretion of the South American frog, Phyllomedusa palliata","abstract":"In recent years, the antibiotic resistance of bacteria has stimulated the development of new antibiotics. Antimicrobial peptides (AMPs) from amphibian skin secretions possess broad-spectrum antimicrobial activities through the mechanism that is unlikely to induce antibiotic resistance. Thus, AMPs are great candidates for new antibiotics. <br/>In this study, the precursor-encoding cDNA sequence of QUB-2652 was identified in the skin secretion of Phyllomedusa palliata by ‘Shotgun’ cloning. Then, QUB-2652 was synthesised by solid phase peptide synthesis (SPPS) according to its translated putative mature peptide sequence. After authenticated by Matrix-assisted laser desorption/ionisation Time-of-flight mass spectrometry and purified by Reversed-phase high performance liquid chromatography, the pure QUB-2652 was finally subjected to some functional tests. <br/>According to the BLAST analysis, QUB-2652 showed high sequence similarity with dermaseptins. Results of functional tests showed that QUB-2652 possessed prominent antimicrobial activities against E. coli, S. aureus and C. albicans with the minimum inhibitory concentrations of 2, 2 and 1 µM, respectively. QUB-2652 also showed strong anti-proliferative effects on NCI-H157, PC-3 and U251MG cell lines. Meanwhile, the haemolytic activity of QUB-2652 on horse erythrocytes was 3.6% at 1 µM and 10.6% at 2 µM. <br/>This study is expected to inspire further studies on peptides from frog skin secretions and provide useful clues for developing new peptide antibiotics and anticancer drugs.","abstract_html":"In recent years, the antibiotic resistance of bacteria has stimulated the development of new antibiotics. Antimicrobial peptides (AMPs) from amphibian skin secretions possess broad-spectrum antimicrobial activities through the mechanism that is unlikely to induce antibiotic resistance. Thus, AMPs are great candidates for new antibiotics. &lt;br/&gt;In this study, the precursor-encoding cDNA sequence of QUB-2652 was identified in the skin secretion of Phyllomedusa palliata by ‘Shotgun’ cloning. Then, QUB-2652 was synthesised by solid phase peptide synthesis (SPPS) according to its translated putative mature peptide sequence. After authenticated by Matrix-assisted laser desorption/ionisation Time-of-flight mass spectrometry and purified by Reversed-phase high performance liquid chromatography, the pure QUB-2652 was finally subjected to some functional tests. &lt;br/&gt;According to the BLAST analysis, QUB-2652 showed high sequence similarity with dermaseptins. Results of functional tests showed that QUB-2652 possessed prominent antimicrobial activities against E. coli, S. aureus and C. albicans with the minimum inhibitory concentrations of 2, 2 and 1 µM, respectively. QUB-2652 also showed strong anti-proliferative effects on NCI-H157, PC-3 and U251MG cell lines. Meanwhile, the haemolytic activity of QUB-2652 on horse erythrocytes was 3.6% at 1 µM and 10.6% at 2 µM. &lt;br/&gt;This study is expected to inspire further studies on peptides from frog skin secretions and provide useful clues for developing new peptide antibiotics and anticancer drugs.","abstract_has_math":false,"creators":["Dong, Ziyi"],"institution":"Queen's University Belfast","degree_name":"Master of Philosophy","degree_level":"Masters Thesis","degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":["Wang, Lei","Chen, Tianbao","Shaw, Christopher"],"committee_chairs":[],"committee_members":[],"year":2018,"date_issued":"2018-7","date_published":"2018-7","updated_at":"2026-07-24T03:54:53Z","subjects":[],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["oai:pure.qub.ac.uk/portal:studenttheses/aff69d08-c0ad-4108-81bd-5d6d86682fd4"],"render_values":[{"text":"oai:pure.qub.ac.uk/portal:studenttheses/aff69d08-c0ad-4108-81bd-5d6d86682fd4","href":null,"code":true}]}]},"links":{"outbound_url":"https://pure.qub.ac.uk/en/studentTheses/aff69d08-c0ad-4108-81bd-5d6d86682fd4","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["Wang, Lei","Chen, Tianbao","Shaw, Christopher"]},{"key":"dc:creator","label":"Author","values":["Dong, Ziyi"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2018-7"]},{"key":"dc:date.issued","label":"Date","values":["2018-7"]},{"key":"dc:publisher.department","label":"Dc Publisher Department","values":["School of Pharmacy"]},{"key":"dc:publisher.institution","label":"Dc Publisher Institution","values":["Queen's University Belfast"]},{"key":"dc:relation.isreferencedby","label":"Dc Relation Isreferencedby","values":["https://pure.qub.ac.uk/en/studentTheses/aff69d08-c0ad-4108-81bd-5d6d86682fd4"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]},{"key":"dc:type.qualificationlevel","label":"Dc Type Qualificationlevel","values":["Masters Thesis"]},{"key":"dc:type.qualificationname","label":"Dc Type Qualificationname","values":["Master of Philosophy"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["eng"]},{"key":"dc:rights.embargodate","label":"Dc Rights Embargodate","values":["2023-10-31"]},{"key":"dc:rights.embargoreason","label":"Dc Rights Embargoreason","values":["/dk/atira/pure/core/document/studentthesisembargoreason/publicationissues"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["oai:pure.qub.ac.uk/portal:studenttheses/aff69d08-c0ad-4108-81bd-5d6d86682fd4","https://pure.qub.ac.uk/en/studentTheses/aff69d08-c0ad-4108-81bd-5d6d86682fd4"]},{"key":"dc:identifier.uri","label":"Identifier URI","values":["https://pure.qub.ac.uk/files/157905131/DONG_ZIYI_THESIS.pdf"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["In recent years, the antibiotic resistance of bacteria has stimulated the development of new antibiotics. Antimicrobial peptides (AMPs) from amphibian skin secretions possess broad-spectrum antimicrobial activities through the mechanism that is unlikely to induce antibiotic resistance. Thus, AMPs are great candidates for new antibiotics. <br/>In this study, the precursor-encoding cDNA sequence of QUB-2652 was identified in the skin secretion of Phyllomedusa palliata by ‘Shotgun’ cloning. Then, QUB-2652 was synthesised by solid phase peptide synthesis (SPPS) according to its translated putative mature peptide sequence. After authenticated by Matrix-assisted laser desorption/ionisation Time-of-flight mass spectrometry and purified by Reversed-phase high performance liquid chromatography, the pure QUB-2652 was finally subjected to some functional tests. <br/>According to the BLAST analysis, QUB-2652 showed high sequence similarity with dermaseptins. Results of functional tests showed that QUB-2652 possessed prominent antimicrobial activities against E. coli, S. aureus and C. albicans with the minimum inhibitory concentrations of 2, 2 and 1 µM, respectively. QUB-2652 also showed strong anti-proliferative effects on NCI-H157, PC-3 and U251MG cell lines. Meanwhile, the haemolytic activity of QUB-2652 on horse erythrocytes was 3.6% at 1 µM and 10.6% at 2 µM. <br/>This study is expected to inspire further studies on peptides from frog skin secretions and provide useful clues for developing new peptide antibiotics and anticancer drugs."]},{"key":"dc:title","label":"Title","values":["The discovery and bioactivity evaluation of a novel peptide, QUB-2652, from the skin secretion of the South American frog, Phyllomedusa palliata"]}]}],"canonical_facts":{"dc:contributor.advisor":["Wang, Lei","Chen, Tianbao","Shaw, Christopher"],"dc:creator":["Dong, Ziyi"],"dc:date":["2018-7"],"dc:date.issued":["2018-7"],"dc:description.abstract":["In recent years, the antibiotic resistance of bacteria has stimulated the development of new antibiotics. Antimicrobial peptides (AMPs) from amphibian skin secretions possess broad-spectrum antimicrobial activities through the mechanism that is unlikely to induce antibiotic resistance. Thus, AMPs are great candidates for new antibiotics. <br/>In this study, the precursor-encoding cDNA sequence of QUB-2652 was identified in the skin secretion of Phyllomedusa palliata by ‘Shotgun’ cloning. Then, QUB-2652 was synthesised by solid phase peptide synthesis (SPPS) according to its translated putative mature peptide sequence. After authenticated by Matrix-assisted laser desorption/ionisation Time-of-flight mass spectrometry and purified by Reversed-phase high performance liquid chromatography, the pure QUB-2652 was finally subjected to some functional tests. <br/>According to the BLAST analysis, QUB-2652 showed high sequence similarity with dermaseptins. Results of functional tests showed that QUB-2652 possessed prominent antimicrobial activities against E. coli, S. aureus and C. albicans with the minimum inhibitory concentrations of 2, 2 and 1 µM, respectively. QUB-2652 also showed strong anti-proliferative effects on NCI-H157, PC-3 and U251MG cell lines. Meanwhile, the haemolytic activity of QUB-2652 on horse erythrocytes was 3.6% at 1 µM and 10.6% at 2 µM. <br/>This study is expected to inspire further studies on peptides from frog skin secretions and provide useful clues for developing new peptide antibiotics and anticancer drugs."],"dc:identifier":["oai:pure.qub.ac.uk/portal:studenttheses/aff69d08-c0ad-4108-81bd-5d6d86682fd4","https://pure.qub.ac.uk/en/studentTheses/aff69d08-c0ad-4108-81bd-5d6d86682fd4"],"dc:identifier.uri":["https://pure.qub.ac.uk/files/157905131/DONG_ZIYI_THESIS.pdf"],"dc:language":["eng"],"dc:publisher.department":["School of Pharmacy"],"dc:publisher.institution":["Queen's University Belfast"],"dc:relation.isreferencedby":["https://pure.qub.ac.uk/en/studentTheses/aff69d08-c0ad-4108-81bd-5d6d86682fd4"],"dc:rights.embargodate":["2023-10-31"],"dc:rights.embargoreason":["/dk/atira/pure/core/document/studentthesisembargoreason/publicationissues"],"dc:title":["The discovery and bioactivity evaluation of a novel peptide, QUB-2652, from the skin secretion of the South American frog, Phyllomedusa palliata"],"dc:type":["Thesis"],"dc:type.qualificationlevel":["Masters Thesis"],"dc:type.qualificationname":["Master of Philosophy"]},"updated_at":"2026-07-24T03:54:53Z"}