{"id":{"repo_id":"qu-belfast","oai_identifier":"oai:pure.qub.ac.uk/portal:studenttheses/c8f3c239-cef5-4384-9869-88777f4a0209"},"canonical_url":"https://search.dev.ndltd.org/etd/qu-belfast/oai:pure.qub.ac.uk/portal:studenttheses/c8f3c239-cef5-4384-9869-88777f4a0209","repository":{"repo_id":"qu-belfast","name":"Queen's University Belfast","base_url":"https://pureadmin.qub.ac.uk/ws/oai"},"display":{"title":"QUB-1453: A Bioactive Peptide from the Defensive Skin Secretion of Rana amurensis","abstract":"Amphibian skin secretion is one of the richest sources for antimicrobial peptides (AMPs) which have potent bioactivity and pharmaceutical value for new drug development. In this thesis, QUB-1452, an AMP, was isolated and characterised from the skin secretion of Rana amurensis. The peptide is composed of 13 amino acid residues, FLPVLISLIGRLL, and is C-terminally amidated. The structure and functions of QUB-1452 were identified via nucleotide/amino acid sequencing and bioactivity analyses. The results showed that QUB-1452 had relatively strong antimicrobial activity against S. aureus (Staphylococcus aureus) and C. albicans (Candida albicans) with minimal inhibitory concentrations of 8 µmol/L and 16 µmol/L respectively, while it had little effect on the growth of E. coli (Escherichia coli). In addition, QUB-1452 had high haemolytic activity at high concentrations, whereas the haemolytic activity was relatively low at the minimal inhibitory concentrations against S. aureus and C. albicans at 3.3% and 6.6%, respectively. Moreover, the peptide had no effect on cancer cells. These data demonstrate the potential of amphibian skin secretions to provide novel natural peptide templates for biological evaluation.","abstract_html":"Amphibian skin secretion is one of the richest sources for antimicrobial peptides (AMPs) which have potent bioactivity and pharmaceutical value for new drug development. In this thesis, QUB-1452, an AMP, was isolated and characterised from the skin secretion of Rana amurensis. The peptide is composed of 13 amino acid residues, FLPVLISLIGRLL, and is C-terminally amidated. The structure and functions of QUB-1452 were identified via nucleotide/amino acid sequencing and bioactivity analyses. The results showed that QUB-1452 had relatively strong antimicrobial activity against S. aureus (Staphylococcus aureus) and C. albicans (Candida albicans) with minimal inhibitory concentrations of 8 µmol/L and 16 µmol/L respectively, while it had little effect on the growth of E. coli (Escherichia coli). In addition, QUB-1452 had high haemolytic activity at high concentrations, whereas the haemolytic activity was relatively low at the minimal inhibitory concentrations against S. aureus and C. albicans at 3.3% and 6.6%, respectively. Moreover, the peptide had no effect on cancer cells. These data demonstrate the potential of amphibian skin secretions to provide novel natural peptide templates for biological evaluation.","abstract_has_math":false,"creators":["Li, Dawei"],"institution":"Queen's University Belfast","degree_name":"Master of Philosophy","degree_level":"Masters Thesis","degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":["Shaw, Christopher","Chen, Tianbao","Zhou, Mei","Wang, Lei"],"committee_chairs":[],"committee_members":[],"year":2017,"date_issued":"2017-8-29","date_published":"2017-8-29","updated_at":"2026-07-24T03:54:46Z","subjects":[],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["oai:pure.qub.ac.uk/portal:studenttheses/c8f3c239-cef5-4384-9869-88777f4a0209"],"render_values":[{"text":"oai:pure.qub.ac.uk/portal:studenttheses/c8f3c239-cef5-4384-9869-88777f4a0209","href":null,"code":true}]}]},"links":{"outbound_url":"https://pure.qub.ac.uk/en/studentTheses/c8f3c239-cef5-4384-9869-88777f4a0209","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["Shaw, Christopher","Chen, Tianbao","Zhou, Mei","Wang, Lei"]},{"key":"dc:creator","label":"Author","values":["Li, Dawei"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2017-8-29"]},{"key":"dc:date.issued","label":"Date","values":["2017-8-29"]},{"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/c8f3c239-cef5-4384-9869-88777f4a0209"]},{"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":["2022-09-01"]},{"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/c8f3c239-cef5-4384-9869-88777f4a0209","https://pure.qub.ac.uk/en/studentTheses/c8f3c239-cef5-4384-9869-88777f4a0209"]},{"key":"dc:identifier.uri","label":"Identifier URI","values":["https://pure.qub.ac.uk/files/135271760/Li_Dawei_Thesis.pdf"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Amphibian skin secretion is one of the richest sources for antimicrobial peptides (AMPs) which have potent bioactivity and pharmaceutical value for new drug development. In this thesis, QUB-1452, an AMP, was isolated and characterised from the skin secretion of Rana amurensis. The peptide is composed of 13 amino acid residues, FLPVLISLIGRLL, and is C-terminally amidated. The structure and functions of QUB-1452 were identified via nucleotide/amino acid sequencing and bioactivity analyses. The results showed that QUB-1452 had relatively strong antimicrobial activity against S. aureus (Staphylococcus aureus) and C. albicans (Candida albicans) with minimal inhibitory concentrations of 8 µmol/L and 16 µmol/L respectively, while it had little effect on the growth of E. coli (Escherichia coli). In addition, QUB-1452 had high haemolytic activity at high concentrations, whereas the haemolytic activity was relatively low at the minimal inhibitory concentrations against S. aureus and C. albicans at 3.3% and 6.6%, respectively. Moreover, the peptide had no effect on cancer cells. These data demonstrate the potential of amphibian skin secretions to provide novel natural peptide templates for biological evaluation."]},{"key":"dc:title","label":"Title","values":["QUB-1453: A Bioactive Peptide from the Defensive Skin Secretion of Rana amurensis"]}]}],"canonical_facts":{"dc:contributor.advisor":["Shaw, Christopher","Chen, Tianbao","Zhou, Mei","Wang, Lei"],"dc:creator":["Li, Dawei"],"dc:date":["2017-8-29"],"dc:date.issued":["2017-8-29"],"dc:description.abstract":["Amphibian skin secretion is one of the richest sources for antimicrobial peptides (AMPs) which have potent bioactivity and pharmaceutical value for new drug development. In this thesis, QUB-1452, an AMP, was isolated and characterised from the skin secretion of Rana amurensis. The peptide is composed of 13 amino acid residues, FLPVLISLIGRLL, and is C-terminally amidated. The structure and functions of QUB-1452 were identified via nucleotide/amino acid sequencing and bioactivity analyses. The results showed that QUB-1452 had relatively strong antimicrobial activity against S. aureus (Staphylococcus aureus) and C. albicans (Candida albicans) with minimal inhibitory concentrations of 8 µmol/L and 16 µmol/L respectively, while it had little effect on the growth of E. coli (Escherichia coli). In addition, QUB-1452 had high haemolytic activity at high concentrations, whereas the haemolytic activity was relatively low at the minimal inhibitory concentrations against S. aureus and C. albicans at 3.3% and 6.6%, respectively. Moreover, the peptide had no effect on cancer cells. 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