| Identification | Back Directory | [Name]
L-Phenylalanyl-L-leucyl-L-prolyl-L-leucyl-L-isoleucylglycyl-L-arginyl-L-valyl-L-leucyl-L-serylglycyl-L-isoleucyl-L-leucinamide | [CAS]
188713-69-1 | [Synonyms]
L-Phenylalanyl-L-leucyl-L-prolyl-L-leucyl-L-isoleucylglycyl-L-arginyl-L-valyl-L-leucyl-L-serylglycyl-L-isoleucyl-L-leucinamide
L-Leucinamide, L-phenylalanyl-L-leucyl-L-prolyl-L-leucyl-L-isoleucylglycyl-L-arginyl-L-valyl-L-leucyl-L-serylglycyl-L-isoleucyl- | [Molecular Formula]
C68H117N17O14 | [MDL Number]
MFCD29042331 | [MOL File]
188713-69-1.mol | [Molecular Weight]
1396.76 |
| Hazard Information | Back Directory | [Uses]
Temporin A is a short alpha-helical antimicrobial peptide isolated from the skin of the frog Rana temporaria. Temporin A is effective against a broad spectrum of Gram-positive bacteria. Temporin A interacts directly with the cell membrane of the microorganism and it is non-toxic to erythrocytes at concentrations that are antimicrobial. Temporin A also has antifungal activities (against yeast-like Candida albicans)[1][1][3]. | [References]
[1] M?ntyl? T, Sirola H, Kansanen E, et al. Effect of temporin A modifications on its cytotoxicity and antimicrobial activity. APMIS. 2005;113(7-8):497-505. DOI:10.1111/j.1600-0463.2005.apm_107.x
[2] Wade D, et al. Antibacterial activities of temporin A analogs. FEBS Lett. 2000;479(1-2):6-9. DOI:10.1016/s0014-5793(00)01754-3
[3] Kamysz W, et al. Temporin A and its retro-analogues: synthesis, conformational analysis and antimicrobial activities. J Pept Sci. 2006;12(8):533-537. DOI:10.1002/psc.762 |
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