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        <identifier>oai:figshare.com:article/32638194</identifier>
        <datestamp>2026-10-01T16:46:59Z</datestamp>
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          <dc:title>Characterisation and bioactivity evaluation of a peptide, Odorrana-S1, from the skin secretion of the frog, Odorrana grahami</dc:title>
          <dc:creator>Zulikala Dilimulati (24168012)</dc:creator>
          <dc:subject>PUREID: 526184547</dc:subject>
          <dc:subject>Antimicrobial peptides</dc:subject>
          <dc:subject>Odorrana grahami</dc:subject>
          <dc:subject>skin secretion</dc:subject>
          <dc:subject>molecular cloning</dc:subject>
          <dc:subject>antimicrobial activity</dc:subject>
          <dc:subject>AMP</dc:subject>
          <dc:description>Amphibian skin secretion is an incredible resource for novel bioactive peptide discovery. Peptides produced from amphibian skin secretion from anuran species demonstrate exceptional antibiotic effects and may ultimately play a central role as alternatives to classical antibiotics as the latter have largely lost their efficacy due to resistance acquisition by target bacteria. &lt;br&gt;&lt;br&gt;In this study, the discovery of a novel peptide is described from the skin secretion of Odorrana grahami and was named Odorrana-S1. It was successfully cloned by “shotgun” cloning and Sanger sequencing established that it was composed of 14 amino acids. Following synthesis through solid phase peptide synthesis, RP-HPLC purification and MALDI-TOF MS analysis, the peptide was deemed to be of sufficiently high purity for biofunctional analysis. After conducting a series of bioassays including MIC, MTT and haemolysis assays, Odorrana-S1 displayed MICs of &gt;512 μM, no significant performance against cancer cells and no haemolysis of horse red blood cells. &lt;br&gt;Although Odorrana-S1 did not demonstrate remarkable bioactivities compared with other natural or synthetic antimicrobial peptides (AMPs), it offered a new insight into the effects of structural and physical properties on biological activity which can aid in the design of antimicrobial peptide analogues.&lt;br&gt;&lt;br&gt;&lt;i&gt;Thesis is embargoed until 31 December 2028.&lt;/i&gt;&lt;br&gt;</dc:description>
          <dc:date>2026-10-01T16:46:59Z</dc:date>
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          <dc:identifier>10.17034/32638194.v1</dc:identifier>
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          <dc:rights>All Rights Reserved</dc:rights>
          <dc:rights>Open Access after 2028-12-31</dc:rights>
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