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| | L-Phenylalanyl-L-leucyl-L-prolyl-L-leucyl-L-isoleucylglycyl-L-arginyl-L-valyl-L-leucyl-L-serylglycyl-L-isoleucyl-L-leucinamide Basic information |
| | L-Phenylalanyl-L-leucyl-L-prolyl-L-leucyl-L-isoleucylglycyl-L-arginyl-L-valyl-L-leucyl-L-serylglycyl-L-isoleucyl-L-leucinamide Chemical Properties |
| density | 1.30±0.1 g/cm3(Predicted) | | pka | 12.94±0.46(Predicted) | | form | Solid | | color | White to off-white |
| | L-Phenylalanyl-L-leucyl-L-prolyl-L-leucyl-L-isoleucylglycyl-L-arginyl-L-valyl-L-leucyl-L-serylglycyl-L-isoleucyl-L-leucinamide Usage And Synthesis |
| 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] Mntyl 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 |
| | L-Phenylalanyl-L-leucyl-L-prolyl-L-leucyl-L-isoleucylglycyl-L-arginyl-L-valyl-L-leucyl-L-serylglycyl-L-isoleucyl-L-leucinamide Preparation Products And Raw materials |
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