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Chemical Compound Review:

Esculentin 1-[3-[5-[5-(3,5-dihydroxy-4- methoxy-6...

Synonyms: AC1L4MQG, AC1Q5CDV, AR-1C0920, A809397, 131889-89-9

Chen, T. et al., Simmaco, M. et al., Simmaco, M. et al., Simmaco, M. et al.

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Disease relevance of Esculentin

In particular, esculentin is the most active against Staphylococcus aureus, and has a much lower hemolytic activity [1].

High impact information on Esculentin

Specific esculentin cDNAs were amplified by 3'-RACE using a degenerate primer designed for a consensus nucleotide sequence in the 5' untranslated region of previously characterized ranid frog peptide cDNAs [2].
A cDNA library from the skin of Rana temporaria has been screened using a cDNA fragment probe that encodes the signal peptide of the precursor of esculentin from the skin secretion of Rana esculenta [3].

Analytical, diagnostic and therapeutic context of Esculentin

Antimicrobial peptides from skin secretions of Rana esculenta. Molecular cloning of cDNAs encoding esculentin and brevinins and isolation of new active peptides [4].

References

Novel antimicrobial peptides from skin secretion of the European frog Rana esculenta. Simmaco, M., Mignogna, G., Barra, D., Bossa, F. FEBS Lett. (1993) [Pubmed]
Cloning from tissue surrogates: Antimicrobial peptide (esculentin) cDNAs from the defensive skin secretions of Chinese ranid frogs. Chen, T., Zhou, M., Chen, W., Lorimer, J., Rao, P., Walker, B., Shaw, C. Genomics (2006) [Pubmed]
Temporins, antimicrobial peptides from the European red frog Rana temporaria. Simmaco, M., Mignogna, G., Canofeni, S., Miele, R., Mangoni, M.L., Barra, D. Eur. J. Biochem. (1996) [Pubmed]
Antimicrobial peptides from skin secretions of Rana esculenta. Molecular cloning of cDNAs encoding esculentin and brevinins and isolation of new active peptides. Simmaco, M., Mignogna, G., Barra, D., Bossa, F. J. Biol. Chem. (1994) [Pubmed]

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