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Temporin-LTb

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Temporin-LTb is an antibacterial peptide isolated from Hylarana latouchii. It has activity against gram-positive bacteria.

Category
Functional Peptides
Catalog number
BAT-011339
Molecular Formula
C77H129N19O16
Molecular Weight
1577.00
IUPAC Name
(S)-6-amino-N-((S)-1-(((S)-1-amino-1-oxo-3-phenylpropan-2-yl)amino)-4-methyl-1-oxopentan-2-yl)-2-((2S,5S,11S,14S,17S,23S,26S,29S,32S)-32-amino-26,29-di((S)-sec-butyl)-11-(3-guanidinopropyl)-2,23-bis((R)-1-hydroxyethyl)-5,17-diisobutyl-14-isopropyl-4,7,10,13,16,19,22,25,28,31-decaoxo-33-phenyl-3,6,9,12,15,18,21,24,27,30-decaazatritriacontanamido)hexanamide
Synonyms
Phe-Ile-Ile-Thr-Gly-Leu-Val-Arg-Gly-Leu-Thr-Lys-Leu-Phe-NH2
Sequence
FIITGLVRGLTKLF-NH2
1. Molecular cloning and characterization of antimicrobial peptides from skin of the broad-folded frog, Hylarana latouchii
Hui Wang, Zhijun Yu, Yuhong Hu, Haining Yu, Ran Ran, Jiangnan Xia, Duo Wang, Shujie Yang, Xiaohong Yang, Jingze Liu Biochimie. 2012 Jun;94(6):1317-26. doi: 10.1016/j.biochi.2012.02.032. Epub 2012 Mar 8.
Seven cDNA sequences encoding antimicrobial peptide (AMP) precursors were cloned by screening the skin-derived cDNA library of the broad-folded frog, Hylarana latouchii. Seven of the deduced peptides are highly similar to AMPs in five families of brevinin-2 (brevinin-2LTa, brevinin-2LTb, and brevinin-2LTc), esculentin-1 (esculentin-1LTa), esculentin-2 (esculentin-2LTa), palustrin-2 (palustrin-2LTa), and temporin (temporin-LTe). The actual sequences and characteristics of mature AMPs were analyzed by RP-HPLC and LC-MS/MS-based proteomics approaches in combination of four different protein digestion processes and by LTQ XL in combination of gas-phase fractionation (GPF) analysis. Moreover, most of the peptides found in this study hardly display hemolytic activity in vitro, suggesting they are promising antimicrobial drug candidates.
2. Isolation, characterization and molecular cloning of new antimicrobial peptides belonging to the brevinin-1 and temporin families from the skin of Hylarana latouchii (Anura: Ranidae)
Hui Wang, Xiuwen Yan, Haining Yu, Yuhong Hu, Zhijun Yu, Hongyuan Zheng, Ze Chen, Zhiping Zhang, Jingze Liu Biochimie. 2009 Apr;91(4):540-7. doi: 10.1016/j.biochi.2009.01.007.
Around 40 species of Hylarana amphibians are distributed in tropical and subtropical Asia, and Chinese broad-folded frog, Hylarana latouchii (Boulenger, 1899) is one of them. In this study, six different cDNAs encoding four novel antimicrobial peptide precursors were cloned by screening the cDNA library of the Chinese broad-folded frog skin. The protein sequence analysis demonstrated that two deduced peptides belong to the brevinin-1 family, and the other two belong to temporin family of amphibian antimicrobial peptides. Thus, they were named as brevinin-1LT1 (FMGSALRIAAKVLPAALCQIFKKC), brevinin-1LT2 (FFGSVLKVAAKVLPAALCQIFKKC), temporin-LT1 (FLPGLIAGIAKML-NH2) and temporin-LT2 (FLPIALKALGSIFPKIL-NH2), respectively. Furthermore, brevinin-1LT1 and temporin-LT1 were purified by HPLC from the skin secretion of H. latouchii. In this work, all the peptides kill microbes by membrane-disturbing mechanisms, and this procedure was visualized via scanning electron microscopy (SEM).
3. Novel antimicrobial peptides isolated from the skin secretions of Hainan odorous frog, Odorrana hainanensis
Hui Wang, Zhijun Yu, Yuhong Hu, Fengjiao Li, Limeng Liu, Hongyuan Zheng, Hao Meng, Shujie Yang, Xiaolong Yang, Jingze Liu Peptides. 2012 Jun;35(2):285-90. doi: 10.1016/j.peptides.2012.03.007. Epub 2012 Mar 16.
Long time geographical isolation of Hainan Island from the China continent has resulted in appearance of many novel frog species. As one of them, Hainan odorous frog, Odorrana hainanensis possesses some special antimicrobial peptides distinct from those found in other Odorrana. In this study, three antimicrobial peptides have been purified and characterized from the skin secretion of O. hainanensis. With the similarity to the temporin family, two peptides are characterized by amidated C-terminals, so they are named as temporin-HN1 (AILTTLANWARKFL-NH(2)) and temporin-HN2 (NILNTIINLAKKIL-NH(2)). The third antimicrobial peptide belongs to the brevinin-1 family which is widely distributed in Eurasian ranids, and thus, it is named as brevinin-1HN1 (FLPLIASLAANFVPKIFCKITKKC). Furthermore, after sequencing 68 clones, eight cDNAs encoding antimicrobial peptide precursors were cloned from the skin-derived cDNA library of O. hainanensis. These eight cDNAs can encode seven mature antimicrobial peptides including the above three, as well as brevinin-1V, brevinin-2HS2, odorranain-A6, and odorranain-B1. Twelve different species of microorganisms were chosen, including Gram-positive, Gram-negative and fungi, to test the antimicrobial activities of temporin-HN1, temporin-HN2, brevinin-1HN1, brevinin-1V, and brevinin-2HS2. The result shows that, in addition to their activities against Gram-positive bacteria, temporin-HN1 and temporin-HN2 also possess activities against some Gram-negative bacteria and fungi. However, the two antimicrobial peptides, brevinin-1HN1 and brevinin-1V of the brevinin-1 family have stronger antimicrobial activities than temporin-HN1 and temporin-HN2 of the temporin family. Brevinin-1HN1 possesses activity against Staphylococcus aureus (ATCC25923), Rhodococcus rhodochrous X15, and Slime mould 090223 at the concentration of 1.2 μM.
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