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        <datestamp>2026-10-01T17:16:40Z</datestamp>
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          <dc:title>Identification and functional study of a bioactive peptide QUB-2007 from the skin secretion of the bicolour tree-frog Phyllomedusa bicolor</dc:title>
          <dc:creator>Zixin Xu (11966348)</dc:creator>
          <dc:subject>PUREID: 250506515</dc:subject>
          <dc:subject>Antimicrobial peptides</dc:subject>
          <dc:subject>antimicrobial activity</dc:subject>
          <dc:subject>anti-proliferation activity</dc:subject>
          <dc:subject>haemolytic activity</dc:subject>
          <dc:subject>non-small lung cancer cell</dc:subject>
          <dc:subject>phylloseptin</dc:subject>
          <dc:description>Antimicrobial peptides secreted in amphibian skin secretions have many important bioactivities and act as the first line of defence against invading microorganisms. In this thesis, QUB-2007, a peptide belonging to the Phylloseptin family of the Dermaseptin superfamily, was derived from the skin secretion of Phyllomedusa bicolor. The peptide sequence was obtained by molecular cloning through constructing a cDNA library with isolated mRNA from frog skin secretion. The peptide was synthesised by solid phase peptide synthesis, purified using reversed-phase high performance liquid chromatography and structurally-confirmed by MALDI-TOF MS. In broth microdilution assays, QUB-2007 showed antimicrobial activities against the Gram-negative bacterium, Escherichia coli (E. coli ATCC CRM 8739), and the yeast, Candida albicans (C. albicans ATCC CRM 10231) at concentration of 32 μM, and the Gram-positive bacterium, Staphylococcus aureus (S. aureus ATCC CRM6538) at a concentration of 8 μM. In terms of MTT anticancer cell proliferation assays, QUB-2007 was shown to have anticancer activities against HCI-H838 lung cancer cells at a concentration of 10-4 M. With regard to haemolysis, QUB-2007 was haemolytic at concentrations of 32 μM could be 15%.&lt;br&gt;&lt;br&gt;In conclusion, QUB-2007 has potential to be a drug, but its haemolytic activity is a big obstacle. It can be achieved by modifying the peptide, such as in changing certain amino acid sequences to change its cationicity, hydrophobicity and amphipathicity.&lt;br&gt;&lt;br&gt;&lt;i&gt;Thesis embargoed until 31 December 2026&lt;/i&gt;.</dc:description>
          <dc:date>2026-10-01T17:16:40Z</dc:date>
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          <dc:identifier>10.17034/32631801.v1</dc:identifier>
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          <dc:rights>All Rights Reserved</dc:rights>
          <dc:rights>Open Access after 2026-12-31</dc:rights>
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