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Brevinin-2LTa

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Brevinin-2LTa is an antimicrobial peptide found in Hylarana latouchii (Broad-folded frog, China, Asia). It has antibacterial activity against Gram-positive bacteria and Gram-negative bacteria.

Category
Functional Peptides
Catalog number
BAT-012982
Molecular Formula
C133H227N37O38S4
Molecular Weight
3080.74
IUPAC Name
(3S,6S,9S,12S,18S,21S,24S,27S)-27-(((2S,8S,11S,14S,17S,20S,23S,26S,29S)-32-amino-20-(2-amino-2-oxoethyl)-11-(4-aminobutyl)-29-(((4R,7S,13S,16S,19S,22R)-7,19-bis(4-aminobutyl)-4-carboxy-13-(hydroxymethyl)-16-isobutyl-6,9,12,15,18,21-hexaoxo-1,2-dithia-5,8,11,14,17,20-hexaazacyclotricosan-22-yl)carbamoyl)-14,17-diisobutyl-26-methyl-8,23-bis(2-(methylthio)ethyl)-3,6,9,12,15,18,21,24,27,32-decaoxo-4,7,10,13,16,19,22,25,28-nonaazadotriacontan-2-yl)carbamoyl)-3-(2-((S)-2-((S)-2-(2-aminoacetamido)propanamido)-3-phenylpropanamido)acetamido)-12,24-bis(4-aminobutyl)-6,9-diisobutyl-18-isopropyl-21-methyl-4,7,10,13,16,19,22,25-octaoxo-5,8,11,14,17,20,23,26-octaazatriacontanedioic acid
Synonyms
Gly-Ala-Phe-Gly-Asp-Leu-Leu-Lys-Gly-Val-Ala-Lys-Glu-Ala-Gly-Met-Lys-Leu-Leu-Asn-Met-Ala-Gln-Cys-Lys-Leu-Ser-Gly-Lys-Cys (Disulfide bridge: Cys24-Cys30)
Appearance
Powder
Purity
>97%
Sequence
GAFGDLLKGVAKEAGMKLLNMAQCKLSGKC (Disulfide bridge: Cys24-Cys30)
Storage
Store at -20°C
1. Identification and characterization of antimicrobial peptides from skin of Amolops ricketti (Anura: Ranidae)
Hui Wang, Ran Ran, Haining Yu, Zhijun Yu, Yuhong Hu, Hongyuan Zheng, Duo Wang, Fan Yang, Renjie Liu, Jingze Liu Peptides. 2012 Jan;33(1):27-34. doi: 10.1016/j.peptides.2011.10.030. Epub 2011 Nov 11.
As one of large amphibian group, there are a total of 45 species of Amolops in the world. However, the antimicrobial peptides (AMPs) existing in this genus has not been extensively studied. In this study, cDNAs encoding five novel AMP precursors were cloned by screening the skin-derived cDNA library of Amolops ricketti, a frog species that exists in southern and western parts of China. Protein sequence analysis led to the identification of five deduced peptides, three belonging to the brevinin-1 family and two belonging to the brevinin-2 family of amphibian AMPs. Thus, they were named as brevinin-1RTa (FLPLLAGVVANFLPQIICKIARKC), brevinin-1RTb (FLGSLLGLVGKVVPTLFCKISKKC), brevinin-1RTc (FLGSLLGLVGKIVPTLICKISKKC), brevinin-2RTa (GLMSTLKDFGKTAAKEIAQSLLSTASCKLAKTC), and brevinin-2RTb (GILDTLKEFGKTAAKGIAQSLLSTASCKLAKTC), respectively. The purification of brevinin-1RTa, brevinin-1RTb, and brevinin-2RTb was carried out by RP-HPLC, and confirmed by the LC-MS/MS-based proteomics approach. All of the peptides displayed different antimicrobial potency against a variety of microorganisms. In addition, brevinin-2RTa and brevinin-2RTb were found to have relatively low hemolytic activity (>400μg/ml) against mammalian red blood cells in vitro, which could potentially be as candidates for developing novel anti-infection agents.
2. The novel antimicrobial peptides from skin of Chinese broad-folded frog, Hylarana latouchii (Anura:Ranidae)
Hui Wang, Yi Lu, Xiuqing Zhang, Yuhong Hu, Haining Yu, Jingze Liu, Junshe Sun Peptides. 2009 Feb;30(2):273-82. doi: 10.1016/j.peptides.2008.10.016. Epub 2008 Nov 5.
Broad-folded frogs (Hylarana latouchii), one member of 12 species of the genus Hylarana in the Chinese frog fauna, are widely distributed in the South of China. In this study, we purified and characterized three antimicrobial peptides from the skin secretion of H. latouchii. Five different cDNA fragments encoding the precursors of these antimicrobial peptides were cloned, and five mature antimicrobial peptides belonging to two different families were deduced from the five cDNAs. Structural characterization of the mature peptides had identified them as members of the brevinin-1 and temporin families. They were named brevinin-1LTa (FFGTALKIAANVLPTAICKILKKC), brevinin-1LTb (FFGTALKIAANILPTAICKILKKC), temporin-LTa (FFPLVLGALGSILPKIF-NH(2)), temporin-LTb (FIITGLVRGLTKLF-NH(2)) and temorin-LTc (SLSRFLSFLKIVYPPAF-NH(2)). Brevinin-1LTa, temporin-LTa, temporin-LTb and temporin-LTc with different antimicrobial activities induced significant morphological alterations of the tested microbial surfaces as shown by scanning electron microscopy, which indicated strong membrane disruption.
3. Characterization of diverse antimicrobial peptides in skin secretions of Chungan torrent frog Amolops chunganensis
Xiaohong Yang, Jiangnan Xia, Zhijun Yu, Yuhong Hu, Fengjiao Li, Hao Meng, Shujie Yang, Jingze Liu, Hui Wang Peptides. 2012 Nov;38(1):41-53. doi: 10.1016/j.peptides.2012.08.008. Epub 2012 Aug 19.
We have cloned, synthesized, and characterized 11 novel antimicrobial peptides from a skin derived cDNA library of the Chungan torrent frog, Amolops chunganensis. Seven of the 11 antimicrobial peptides were present in authentic A. chunganensis skin secretions. Sequence analysis indicated that the 11 peptides belonged to the temporin, esculentin-2, palustrin-2, brevinin-1, and brevinin-2 families. The peptides displayed potent antimicrobial activities against several strains of microorganisms. One peptide, brevinin-1CG5, demonstrated antimicrobial activity against all tested Gram-positive and Gram-negative bacteria and fungi, and showed high antimicrobial potency (MIC=0.6 μM) against Gram-positive bacterium Rhodococcus rhodochrous. Some peptides also demonstrated weak hemolytic activity against human erythrocytes in vitro. Phylogenetic analysis based on the amino acid sequences of brevinin-1, brevinin-2, and esculentin-2 peptides from family Ranidae confirmed that the current taxonomic status of A. chunganensis is correct.
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