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        <identifier>oai:figshare.com:article/32640177</identifier>
        <datestamp>2026-10-01T16:33:30Z</datestamp>
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          <dc:title>Characterisation and therapeutic potential of QUB-1460: an antimicrobial peptide from &lt;i&gt;Rana pleuraden&lt;/i&gt;</dc:title>
          <dc:creator>Xiangyang Lyu (24169116)</dc:creator>
          <dc:subject>PUREID: 613662554</dc:subject>
          <dc:subject>antimicrobial activity</dc:subject>
          <dc:subject>antimicrobial peptides</dc:subject>
          <dc:subject>bioactive compounds</dc:subject>
          <dc:subject>frog skin secretions</dc:subject>
          <dc:subject>Rana pleuraden</dc:subject>
          <dc:description>Antimicrobial peptides (AMPs) from amphibian skin secretions, such as those from the frog Rana pleuraden, have attracted significant interest for their potential therapeutic applications due to the growing challenge of antibiotic resistance, leading to infections that are increasingly difficult to treat. This study focused on QUB-1460, a novel peptide from the Rana pleuraden identified as a member of the pleurain family. Through 'shotgun' cloning and high-performance liquid chromatography (HPLC), the mature peptide sequence was discovered and purified. QUB-1460 demonstrated notable antimicrobial efficacy, particularly against S. aureus, with a minimum inhibitory concentration (MIC) and minimum bactericidal concentration (MBC) at 32 µM, indicating strong bactericidal properties. However, its activity was less pronounced against E. coli (MIC of 128 µM, MBC of 256 µM), and it was largely ineffective against C. albicans at concentrations up to 256 µM. Additionally, QUB-1460 exhibited moderate antiproliferative effects on the NCI-H838 lung cancer cell line, with an IC50 of 22.79 µM, suggesting potential as an anticancer agent. The peptide's structure, characterised by moderate hydrophobicity and a net positive charge, forms an α-helix, contributing to its membrane-disruptive activities. Despite its therapeutic potential, the peptide also displayed haemolytic activity at higher concentrations (40% haemolysis at 64 µM), underlining the need for further structural optimisation to enhance its selectivity and reduce cytotoxicity. Further research will aim to manipulate the peptide structure to attenuate its haemolytic effects while enhancing its antimicrobial and antiproliferative capabilities. Understanding the detailed mechanisms by which QUB-1460 interacts with microbial and cancer cell membranes could lead to novel insights into peptide design for therapeutic purposes. Future research will also explore the synergistic effects of QUB-1460 with conventional antibiotics to enhance their efficacy and potentially reduce the dosage required, addressing the issue of antibiotic resistance more effectively.&lt;br&gt;&lt;br&gt;&lt;i&gt;Thesis is embargoed until 31st December 2029&lt;/i&gt;.&lt;br&gt;&lt;br&gt;</dc:description>
          <dc:date>2026-10-01T16:33:30Z</dc:date>
          <dc:type>Text</dc:type>
          <dc:type>Thesis</dc:type>
          <dc:identifier>10.17034/32640177.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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