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        <datestamp>2026-10-01T16:34:43Z</datestamp>
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          <dc:title>The discovery, rational design, and bioactivity evaluation of antimicrobial peptides from the skin secretions of amphibians</dc:title>
          <dc:creator>Jiachen Liu (4639738)</dc:creator>
          <dc:subject>PUREID: 612159890</dc:subject>
          <dc:subject>antimicrobial peptides</dc:subject>
          <dc:subject>peptide design</dc:subject>
          <dc:subject>molecular cloning</dc:subject>
          <dc:description>Antimicrobial peptides from natural organisms have been extensively studied in recent years.
Their clinical potential is getting stronger as more new peptides are discovered and modified
peptides are designed. A large proportion of antimicrobial peptides have now entered clinical
trials. In Chapter 3, BLP-7S and Bombinin-H2L were extracted from the skin secretions of
Bombina variegata. They both have good antimicrobial activity, but Bombinin-H2L is less
biologically safe and has potential for continued modification. In Chapter 4, a series of analogues
were designed on the basis of Bombinin-H2L. Their main activity and toxicity were affected by
hydrophobicity, which significantly increased their safety when hydrophobicity was reduced to
the safety threshold. When hydrophobicity is reduced to a safe level, increasing the positive
charge significantly improves the antimicrobial activity without increasing haemolysis. The best
results were obtained with BH2L-8R15R and BH2L-78K, a modified peptide with multiple
bactericidal mechanisms. In Chapter 5, to investigate the impact of different living habits on the
activity of antimicrobial peptides secreted by frogs, a specific species of tree frog was selected
as the research subject. QUB-2048 extracted from the skin secretion of Phyllomedusa
hypochondrialis azurea, was modified. This is an antimicrobial peptide of similar length to
Bombinin-H2L. The effect of the common modified peptide residues “-PRW-” on the biological
activity and spatial structure of this peptide was explored. This will lay the foundation for the
rational design of similar peptides of the same family in the future. &lt;br&gt;&lt;i&gt;&lt;br&gt;Thesis is embargoed until 31 December 2029.&lt;/i&gt;</dc:description>
          <dc:date>2026-10-01T16:34:43Z</dc:date>
          <dc:type>Text</dc:type>
          <dc:type>Thesis</dc:type>
          <dc:identifier>10.17034/32640048.v1</dc:identifier>
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          <dc:rights>All Rights Reserved</dc:rights>
          <dc:rights>Open Access after 2029-12-31</dc:rights>
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