Discovery and functional study of a bioactive peptide QUB-1892 from the defensive skin secretion of The Edible Frog (Pelophylax eculentus)
type: CreativeWork
description: 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: 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.
author: Ye, Siyu
language: eng
keywords: peptide, trypsin inhibitor, AMPs
date published: 2020-12
date modified: 2026-07-24T03:55:31Z
provider: Queen's University Belfast
publisher: Networked Digital Library of Theses and Dissertations
type: WebPage
source organization: Queen's University Belfast