{"id":{"repo_id":"qu-belfast","oai_identifier":"oai:pure.qub.ac.uk/portal:studenttheses/8e5a9832-0376-4eef-a8b6-33ee80bc760c"},"canonical_url":"https://search.dev.ndltd.org/etd/qu-belfast/oai:pure.qub.ac.uk/portal:studenttheses/8e5a9832-0376-4eef-a8b6-33ee80bc760c","repository":{"repo_id":"qu-belfast","name":"Queen's University Belfast","base_url":"https://pureadmin.qub.ac.uk/ws/oai"},"display":{"title":"Discovery and functional study of a bioactive peptide QUB-1892 from the defensive skin secretion of The Edible Frog (Pelophylax eculentus)","abstract":"Amphibian skin secretions not only act as mere tegmental lubrication but also have many more complex functions such as seen in their antimicrobial activity. In this thesis, a novel Kunitz-like trypsin inhibitor was isolated from the skin secretion of Pelophylax kl esculentus and was named QUB-1892. The mature peptide was synthesised by solid-phase peptide synthesis (SPPS). RP-HPLC and MALDI-TOF MS were used to purify and analyse the mature peptide. Its minimal inhibitory concentration (MIC) was obtained by using different micro-organisms and its haemolytic activity was tested by the use of horse red blood cells. The results of antimicrobial experiments showed that QUB-1892 was active only against E.coli with a MIC of 256 μM. Trypsin inhibitor assays revealed that QUB-1892 had inhibitory action against trypsin with a Ki value of 3.6 µM. Also, QUB-1892 had low haemolytic activity. The outstanding ability of QUB-1892 to inhibit trypsin gives this novel peptide potential for use in the development of new drugs for clinical application.","abstract_html":"Amphibian skin secretions not only act as mere tegmental lubrication but also have many more complex functions such as seen in their antimicrobial activity. In this thesis, a novel Kunitz-like trypsin inhibitor was isolated from the skin secretion of Pelophylax kl esculentus and was named QUB-1892. The mature peptide was synthesised by solid-phase peptide synthesis (SPPS). RP-HPLC and MALDI-TOF MS were used to purify and analyse the mature peptide. Its minimal inhibitory concentration (MIC) was obtained by using different micro-organisms and its haemolytic activity was tested by the use of horse red blood cells. The results of antimicrobial experiments showed that QUB-1892 was active only against E.coli with a MIC of 256 μM. Trypsin inhibitor assays revealed that QUB-1892 had inhibitory action against trypsin with a Ki value of 3.6 µM. Also, QUB-1892 had low haemolytic activity. The outstanding ability of QUB-1892 to inhibit trypsin gives this novel peptide potential for use in the development of new drugs for clinical application.","abstract_has_math":false,"creators":["Ye, Siyu"],"institution":"Queen's University Belfast","degree_name":"Master of Philosophy","degree_level":"Masters Thesis","degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":["Zhou, Mei","Wang, Lei","Chen, Tianbao"],"committee_chairs":[],"committee_members":[],"year":2020,"date_issued":"2020-12","date_published":"2020-12","updated_at":"2026-07-24T03:55:31Z","subjects":["peptide","trypsin inhibitor","AMPs"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["oai:pure.qub.ac.uk/portal:studenttheses/8e5a9832-0376-4eef-a8b6-33ee80bc760c"],"render_values":[{"text":"oai:pure.qub.ac.uk/portal:studenttheses/8e5a9832-0376-4eef-a8b6-33ee80bc760c","href":null,"code":true}]}]},"links":{"outbound_url":"https://pure.qub.ac.uk/en/studentTheses/8e5a9832-0376-4eef-a8b6-33ee80bc760c","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["Zhou, Mei","Wang, Lei","Chen, Tianbao"]},{"key":"dc:creator","label":"Author","values":["Ye, Siyu"]}]},{"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/8e5a9832-0376-4eef-a8b6-33ee80bc760c"]},{"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":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["peptide","trypsin inhibitor","AMPs"]}]},{"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/8e5a9832-0376-4eef-a8b6-33ee80bc760c","https://pure.qub.ac.uk/en/studentTheses/8e5a9832-0376-4eef-a8b6-33ee80bc760c"]},{"key":"dc:identifier.uri","label":"Identifier URI","values":["https://pure.qub.ac.uk/files/219939945/Discovery_and_functional_study_of_a_bioactive_peptide_QUB_1892_from_the_defensive_skin_secretion_of_The_Edible_Frog_Pelophylax_eculentus_.pdf"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Amphibian skin secretions not only act as mere tegmental lubrication but also have many more complex functions such as seen in their antimicrobial activity. In this thesis, a novel Kunitz-like trypsin inhibitor was isolated from the skin secretion of Pelophylax kl esculentus and was named QUB-1892. The mature peptide was synthesised by solid-phase peptide synthesis (SPPS). RP-HPLC and MALDI-TOF MS were used to purify and analyse the mature peptide. Its minimal inhibitory concentration (MIC) was obtained by using different micro-organisms and its haemolytic activity was tested by the use of horse red blood cells. The results of antimicrobial experiments showed that QUB-1892 was active only against E.coli with a MIC of 256 μM. Trypsin inhibitor assays revealed that QUB-1892 had inhibitory action against trypsin with a Ki value of 3.6 µM. Also, QUB-1892 had low haemolytic activity. The outstanding ability of QUB-1892 to inhibit trypsin gives this novel peptide potential for use in the development of new drugs for clinical application."]},{"key":"dc:title","label":"Title","values":["Discovery and functional study of a bioactive peptide QUB-1892 from the defensive skin secretion of The Edible Frog (Pelophylax eculentus)"]}]}],"canonical_facts":{"dc:contributor.advisor":["Zhou, Mei","Wang, Lei","Chen, Tianbao"],"dc:creator":["Ye, Siyu"],"dc:date":["2020-12"],"dc:date.issued":["2020-12"],"dc:description.abstract":["Amphibian skin secretions not only act as mere tegmental lubrication but also have many more complex functions such as seen in their antimicrobial activity. In this thesis, a novel Kunitz-like trypsin inhibitor was isolated from the skin secretion of Pelophylax kl esculentus and was named QUB-1892. The mature peptide was synthesised by solid-phase peptide synthesis (SPPS). RP-HPLC and MALDI-TOF MS were used to purify and analyse the mature peptide. Its minimal inhibitory concentration (MIC) was obtained by using different micro-organisms and its haemolytic activity was tested by the use of horse red blood cells. The results of antimicrobial experiments showed that QUB-1892 was active only against E.coli with a MIC of 256 μM. Trypsin inhibitor assays revealed that QUB-1892 had inhibitory action against trypsin with a Ki value of 3.6 µM. Also, QUB-1892 had low haemolytic activity. 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