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    <ns1:title language="en">Peptidomic analysis of the host-defense peptides in skin secretions of the Amazon River frog Lithobates palmipes (Ranidae)</ns1:title>
    <ns1:language>en</ns1:language>
    <ns1:description language="en">Skin secretions of certain frog species represent a source of host-defense peptides (HDPs) with therapeutic potential and their primary structures provide insight into taxonomic and phylogenetic relationships. Peptidomic analysis was used to characterize the HDPs in norepinephrine-stimulated skin secretions from the Amazon River frog Lithobates palmipes (Ranidae) collected in Trinidad. A total of ten peptides were purified and identified on the basis of amino acid similarity as belonging to the ranatuerin-2 family (ranatuerin-2PMa, -2PMb, -2PMc, and-2PMd), the brevinin-1 family (brevinin-1PMa, -1PMb, -1PMc and des(8-14)brevinin-1PMa) and the temporin family (temporin-PMa in C-terminally amidated and non-amidated forms). Deletion of the sequence VAAKVLP from brevinin-1PMa (FLPLIAGVAAKVLPKIFCAISKKC) in des[(8-14)brevinin-1PMa resulted in a 10-fold decrease in potency against Staphylococcus aureus (MIC = 31 μM compared with 3 μM) and a &gt; 50-fold decrease in hemolytic activity but potency against Echerichia coli was maintained (MIC = 62.5 μM compared with 50 μM). Temporin-PMa (FLPFLGKLLSGIF.NH2) inhibited growth of S. aureus (MIC = 16 μM) but the non-amidated form of the peptide lacked antimicrobial activity. Cladistic analysis based upon the primary structures of ranaturerin-2 peptides supports the division of New World frogs of the family Ranidae into the genera Lithobates and Rana. A sister-group relationship between L. palmipes and Warszewitsch&apos;s frog Lithobates warszewitschii is indicated within a clade that includes the Tarahumara frog Lithobates tarahumarae. The study has provided further evidence that peptidomic analysis of HDPs in frog skin secretions is a valuable approach to elucidation of the evolutionary history of species within a particular genus.</ns1:description>
    <ns1:keyword language="en">Antimicrobial Peptides; Phylogeny; Amphibia; Proline; Tree</ns1:keyword>
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      <ns2:resource>1552099</ns2:resource>
      <ns2:identifier>10.1016/j.cbd.2023.101069</ns2:identifier>
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        <ns3:firstname>Milena</ns3:firstname>
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        <ns3:institution>University of the West Indies</ns3:institution>
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        <ns3:firstname>Gervonne</ns3:firstname>
        <ns3:lastname>Barran</ns3:lastname>
        <ns3:institution>University of the West Indies</ns3:institution>
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        <ns3:firstname>Jolanta</ns3:firstname>
        <ns3:lastname>Kolodziejek</ns3:lastname>
        <ns3:institution>University of Veterinary Medicine Vienna</ns3:institution>
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        <ns3:firstname>Laurent</ns3:firstname>
        <ns3:lastname>Coquet</ns3:lastname>
        <ns3:institution>Université de Rouen Normandie</ns3:institution>
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        <ns3:firstname>Jérôme</ns3:firstname>
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        <ns3:institution>Université de Rouen Normandie</ns3:institution>
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        <ns3:firstname>Thierry</ns3:firstname>
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        <ns3:firstname>Norbert</ns3:firstname>
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        <ns3:institution>University of Veterinary Medicine Vienna / Mohammed Bin Rashid University of Medicine and Health Sciences</ns3:institution>
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        <ns3:firstname>J. Michael</ns3:firstname>
        <ns3:lastname>Conlon</ns3:lastname>
        <ns3:institution>University of Ulster</ns3:institution>
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    <ns12:name_magazine language="en">Comparative Biochemistry and Physiology D - Genomics and Proteomics</ns12:name_magazine>
    <ns12:pagination>7</ns12:pagination>
    <ns12:volume>46</ns12:volume>
    <ns12:publisher>Elsevier</ns12:publisher>
    <ns12:releaseyear>2023</ns12:releaseyear>
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