{"id":{"repo_id":"qu-belfast","oai_identifier":"oai:pure.qub.ac.uk/portal:studenttheses/5006c42e-50d8-49f6-b297-c6111d704a6b"},"canonical_url":"https://search.dev.ndltd.org/etd/qu-belfast/oai:pure.qub.ac.uk/portal:studenttheses/5006c42e-50d8-49f6-b297-c6111d704a6b","repository":{"repo_id":"qu-belfast","name":"Queen's University Belfast","base_url":"https://pureadmin.qub.ac.uk/ws/oai"},"display":{"title":"Identification and functional evaluation of a bioactive peptide QUB-1369 Secreted from the skin of The Common Frog (Rana Temporaria)","abstract":"Antimicrobial peptides (AMPs) are host defence peptides found abundantly in amphibian skin secretions. They have broad antimicrobial spectrum of Gram-positive bacteria, Gram-negative bacteria, fungi and viruses. In this study, skin secretion of the common frog, Rana temporaria, was used to build a cDNA library by mRNA transcription. A cDNA encoding a peptide biosynthetic precursor transcript was consistently cloned from this by “shot-gun” cloning. The precursor peptide sequence was analysed by bioinformatics tools such as NCBI-BLAST, while Uniprot identified the mature peptide sequence (FLPIVGKLLSGLL-NH2). Then, using Fmoc solid -phase peptide synthesis, the peptide chain was assembled stepwise and attached to resin support. After the peptide was assembled, it was removed from the resin to obtain a crude linear peptide. Reverse-phase HPLC was used to obtain a purified peptide and in accordance with its molecular mass obtained by MALDI-TOF MS, the peptide was named QUB-1369. Antimicrobial assays showed that QUB-1369 was active against Gram-positive bacterium, Staphylococcus aureus and the yeast, Candida albicans at concentrations of 8 µM and 128 µM, respectively. It was not active against Gram-negative bacterium, Escherichia coli. Haemolysis assay of QUB-1369 using horse erythrocytes, showed it was active at a concentration of 16 µM. Anticancer assay found a weak inhibition of HCT 116 Human Colon Carcinoma cells at a concentration of 100 µM.","abstract_html":"Antimicrobial peptides (AMPs) are host defence peptides found abundantly in amphibian skin secretions. They have broad antimicrobial spectrum of Gram-positive bacteria, Gram-negative bacteria, fungi and viruses. In this study, skin secretion of the common frog, Rana temporaria, was used to build a cDNA library by mRNA transcription. A cDNA encoding a peptide biosynthetic precursor transcript was consistently cloned from this by “shot-gun” cloning. The precursor peptide sequence was analysed by bioinformatics tools such as NCBI-BLAST, while Uniprot identified the mature peptide sequence (FLPIVGKLLSGLL-NH2). Then, using Fmoc solid -phase peptide synthesis, the peptide chain was assembled stepwise and attached to resin support. After the peptide was assembled, it was removed from the resin to obtain a crude linear peptide. Reverse-phase HPLC was used to obtain a purified peptide and in accordance with its molecular mass obtained by MALDI-TOF MS, the peptide was named QUB-1369. Antimicrobial assays showed that QUB-1369 was active against Gram-positive bacterium, Staphylococcus aureus and the yeast, Candida albicans at concentrations of 8 µM and 128 µM, respectively. It was not active against Gram-negative bacterium, Escherichia coli. Haemolysis assay of QUB-1369 using horse erythrocytes, showed it was active at a concentration of 16 µM. Anticancer assay found a weak inhibition of HCT 116 Human Colon Carcinoma cells at a concentration of 100 µM.","abstract_has_math":false,"creators":["Liu, Haiyi"],"institution":"Queen's University Belfast","degree_name":"Master of Philosophy","degree_level":"Masters Thesis","degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":["Chen, Tianbao","Zhou, Mei","Wang, Lei"],"committee_chairs":[],"committee_members":[],"year":2020,"date_issued":"2020-12","date_published":"2020-12","updated_at":"2026-07-24T03:55:31Z","subjects":[],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["oai:pure.qub.ac.uk/portal:studenttheses/5006c42e-50d8-49f6-b297-c6111d704a6b"],"render_values":[{"text":"oai:pure.qub.ac.uk/portal:studenttheses/5006c42e-50d8-49f6-b297-c6111d704a6b","href":null,"code":true}]}]},"links":{"outbound_url":"https://pure.qub.ac.uk/en/studentTheses/5006c42e-50d8-49f6-b297-c6111d704a6b","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["Chen, Tianbao","Zhou, Mei","Wang, Lei"]},{"key":"dc:creator","label":"Author","values":["Liu, Haiyi"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2020-12"]},{"key":"dc:date.issued","label":"Date","values":["2020-12"]},{"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/5006c42e-50d8-49f6-b297-c6111d704a6b"]},{"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":["2025-12-31"]},{"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/5006c42e-50d8-49f6-b297-c6111d704a6b","https://pure.qub.ac.uk/en/studentTheses/5006c42e-50d8-49f6-b297-c6111d704a6b"]},{"key":"dc:identifier.uri","label":"Identifier URI","values":["https://pure.qub.ac.uk/files/220812334/Identification_and_functional_evaluation_of_a_bioactive_peptide_QUB_1369_Secreted_from_the_skin_of_The_Common_Frog_Rana_Temporaria_.pdf"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Antimicrobial peptides (AMPs) are host defence peptides found abundantly in amphibian skin secretions. They have broad antimicrobial spectrum of Gram-positive bacteria, Gram-negative bacteria, fungi and viruses. In this study, skin secretion of the common frog, Rana temporaria, was used to build a cDNA library by mRNA transcription. A cDNA encoding a peptide biosynthetic precursor transcript was consistently cloned from this by “shot-gun” cloning. The precursor peptide sequence was analysed by bioinformatics tools such as NCBI-BLAST, while Uniprot identified the mature peptide sequence (FLPIVGKLLSGLL-NH2). Then, using Fmoc solid -phase peptide synthesis, the peptide chain was assembled stepwise and attached to resin support. After the peptide was assembled, it was removed from the resin to obtain a crude linear peptide. Reverse-phase HPLC was used to obtain a purified peptide and in accordance with its molecular mass obtained by MALDI-TOF MS, the peptide was named QUB-1369. Antimicrobial assays showed that QUB-1369 was active against Gram-positive bacterium, Staphylococcus aureus and the yeast, Candida albicans at concentrations of 8 µM and 128 µM, respectively. It was not active against Gram-negative bacterium, Escherichia coli. Haemolysis assay of QUB-1369 using horse erythrocytes, showed it was active at a concentration of 16 µM. Anticancer assay found a weak inhibition of HCT 116 Human Colon Carcinoma cells at a concentration of 100 µM."]},{"key":"dc:title","label":"Title","values":["Identification and functional evaluation of a bioactive peptide QUB-1369 Secreted from the skin of The Common Frog (Rana Temporaria)"]}]}],"canonical_facts":{"dc:contributor.advisor":["Chen, Tianbao","Zhou, Mei","Wang, Lei"],"dc:creator":["Liu, Haiyi"],"dc:date":["2020-12"],"dc:date.issued":["2020-12"],"dc:description.abstract":["Antimicrobial peptides (AMPs) are host defence peptides found abundantly in amphibian skin secretions. 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Antimicrobial assays showed that QUB-1369 was active against Gram-positive bacterium, Staphylococcus aureus and the yeast, Candida albicans at concentrations of 8 µM and 128 µM, respectively. It was not active against Gram-negative bacterium, Escherichia coli. Haemolysis assay of QUB-1369 using horse erythrocytes, showed it was active at a concentration of 16 µM. 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