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Caerin-1.6

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Caerin 1.6 was found in Litoria chloris. Caerin 1.6 is an antimicrobial peptide that adopts an alpha helical conformation which can disrupt bacterial membranes.

Category
Functional Peptides
Catalog number
BAT-013585
Sequence
GLFSVLGAVAKHVLPHVVPVIAEK
1. Anurans against SARS-CoV-2: A review of the potential antiviral action of anurans cutaneous peptides
Marjoriane de Amaral, Julia Ienes-Lima Virus Res. 2022 Jul 2;315:198769. doi: 10.1016/j.virusres.2022.198769. Epub 2022 Apr 14.
At the end of 2019, in China, clinical signs and symptoms of unknown etiology have been reported in several patients whose sample sequencing revealed pneumonia caused by the SARS-CoV-2 virus. COVID-19 is a disease triggered by this virus, and in 2020, the World Health Organization declared it a pandemic. Since then, efforts have been made to find effective therapeutic agents against this disease. Identifying novel natural antiviral drugs can be an alternative to treatment. For this reason, antimicrobial peptides secreted by anurans' skin have gained attention for showing a promissory antiviral effect. Hence, this review aimed to elucidate how and which peptides secreted by anurans' skin can be considered therapeutic agents to treat or prevent human viral infectious diseases. Through a literature review, we attempted to identify potential antiviral frogs' peptides to combat COVID-19. As a result, the Magainin-1 and -2 peptides, from the Magainin family, the Dermaseptin-S9, from the Dermaseptin family, and Caerin 1.6 and 1.10, from the Caerin family, are molecules that already showed antiviral effects against SARS-CoV-2 in silico. In addition to these peptides, this review suggests that future studies should use other families that already have antiviral action against other viruses, such as Brevinins, Maculatins, Esculentins, Temporins, and Urumins. To apply these peptides as therapeutic agents, experimental studies with peptides already tested in silico and new studies with other families not tested yet should be considered.
2. New antibiotic caerin 1 peptides from the skin secretion of the Australian tree frog Litoria chloris. Comparison of the activities of the caerin 1 peptides from the genus Litoria
S T Steinborner, G J Currie, J H Bowie, J C Wallace, M J Tyler J Pept Res. 1998 Feb;51(2):121-6. doi: 10.1111/j.1399-3011.1998.tb00629.x.
The skin glands of the tree frog Litoria chloris contain a variety of peptides including four antibacterial peptides of the caerin 1 family. Two of these, caerins 1.6 and 1.7, are also present in the related species Litoria xanthomera. The other two peptides, caerins 1.8 and 1.9, are new. Their sequences are: GLFKVLGSVAKHLLPHVVPVIAEKL-NH2 [Caerin 1.8] and GLFGVLGSIAKHVLPHVVPVIAEKL-NH2 [Caerin 1.9]. Comparison of the skin peptide profiles of L. chloris and L. xanthomera confirms that these species are more closely related to each other than to any other species of the genus Litoria that we have studied. A comparison is made of the antibiotic activities of nine members of the caerin 1 family of peptides isolated from tree frogs of the genus Litoria.
3. New caerin antibacterial peptides from the skin glands of the Australian tree frog Litoria xanthomera
S T Steinborner, R J Waugh, J H Bowie, J C Wallace, M J Tyler, S L Ramsay J Pept Sci. 1997 May-Jun;3(3):181-5. doi: 10.1002/(sici)1099-1387(199705)3:33.0.co;2-k.
The secretion of the skin glands of the 'orange-thighed frog' Litoria xanthomera contains seven peptides. One of these is the know hypotensive peptide caerulein. Two new peptides, caerin 1.6 [GLFSVLGAVAKHVLPHVVPVIAEKL(NH2)], and caerin 1.7 [GLFKVLGSVAKHLLPHVAPVIAEKL(NH2)] show antibacterial properties. Two other peptides lack the first two amino acid residues of caerins 1.6 and 1.7 and show no antibacterial activity. The identification of the peptides in Litoria xanthomera confirms that this species is related to Litoria caerula, Litoria gilleni and Litoria splendida but not as closely as those three species are related to each other.
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