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Palustrin-2AJ1

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Palustrin-2AJ1 is an antimicrobial peptide found in Amolops jingdongensis (Chinese torrent frog), and has broad-spectrum antibacterial activity against a range of Gram-positive and Gram-negative bacteria.

Category
Functional Peptides
Catalog number
BAT-011684
Molecular Formula
C131H224N38O39S3
Molecular Weight
3051.64
IUPAC Name
(3S,6S,9S,12S,15S,18S,21S,24S,27S,30S,33S,36S,39S,42S,45S,48S)-3-(((S)-6-amino-1-(((S)-1-(((S)-1-(((4R,13S,16S,19S,22R)-19-(4-aminobutyl)-4-carboxy-13-((R)-1-hydroxyethyl)-16-isopropyl-6,9,12,15,18,21-hexaoxo-1,2-dithia-5,8,11,14,17,20-hexaazacyclotricosan-22-yl)amino)-5-guanidino-1-oxopentan-2-yl)amino)-4-methyl-1-oxopentan-2-yl)amino)-1-oxohexan-2-yl)carbamoyl)-24,36-bis(2-amino-2-oxoethyl)-48-((S)-2-((S)-2-(2-aminoacetamido)-3-phenylpropanamido)-4-(methylthio)butanamido)-27,39-bis(4-aminobutyl)-6-((S)-sec-butyl)-12,45-bis((R)-1-hydroxyethyl)-9-isobutyl-15,21,33-triisopropyl-18,30,42-trimethyl-5,8,11,14,17,20,23,26,29,32,35,38,41,44,47-pentadecaoxo-4,7,10,13,16,19,22,25,28,31,34,37,40,43,46-pentadecaazapentacontanedioic acid
Synonyms
PL2AJ1; Recombinant Amolops jingdongensis Palustrin-2AJ1; Gly-Phe-Met-Asp-Thr-Ala-Lys-Asn-Val-Ala-Lys-Asn-Val-Ala-Val-Thr-Leu-Ile-Asp-Lys-Leu-Arg-Cys-Lys-Val-Thr-Gly-Gly-Cys (Disulfide bridge: Cys23-Cys29)
Appearance
Lyophilized Powder or Liquid
Purity
≥98%
Sequence
GFMDTAKNVAKNVAVTLIDKLRCKVTGGC (Disulfide bridge: Cys23-Cys29)
Storage
Store at -20°C
1. A new family of antimicrobial peptides from skin secretions of Rana pleuraden
Xu Wang, Yuzhu Song, Jianxu Li, Huan Liu, Xueqing Xu, Ren Lai, Keyun Zhang Peptides. 2007 Oct;28(10):2069-74. doi: 10.1016/j.peptides.2007.07.020. Epub 2007 Jul 22.
While conducting experiments to investigate antimicrobial peptides of amphibians living in the Yunnan-Guizhou region of southwest China, a new family of antimicrobial peptides was identified from skin secretions of the Yunnan frog, Rana pleuraden. Members of the new peptide family named pleurain-As are composed of 26 amino acids with a unique N-terminal sequence (SIIT) and a disulfide-bridged heptapeptide sequence (CRLYNTC). By BLAST search, pleurain-As had no significant similarity to any known peptides. Native and synthetic peptides showed antimicrobial activities against tested microorganisms including Gram-negative and Gram-positive bacteria and fungi. Twenty different cDNAs encoding pleurain-As were cloned from the skin cDNA library of R. pleuraden. The precursors of pleurain-As are composed of 69 amino acid residues including predicted signal peptides, acidic propieces, and cationic mature antimicrobial peptides. The preproregion of pleurain-A precursor comprises a hydrophobic signal peptide of 22 residues followed by an 18 residue acidic propiece which terminates by a typical prohormone processing signal Lys-Arg. The preproregions of precursors are very similar to other amphibian antimicrobial peptide precursors but the mature pleurain-As are different from other antimicrobial peptide families. The remarkable similarity of preproregions of precursors that give rise to very different antimicrobial peptides in distantly related frog species suggests that the corresponding genes form a multigene family originating from a common ancestor. Furthermore, pleurain-As could exert antimicrobial capability against Helicobacter pylori. This is the first report of naturally occurring peptides with anti-H. pylori activity from Rana amphibians.
2. Hainanenins: a novel family of antimicrobial peptides with strong activity from Hainan cascade-frog, Amolops hainanensis
Songyan Zhang, Huanhuan Guo, Fei Shi, Hui Wang, Lili Li, Xudong Jiao, Yipeng Wang, Haining Yu Peptides. 2012 Feb;33(2):251-7. doi: 10.1016/j.peptides.2012.01.014. Epub 2012 Jan 24.
Antimicrobial peptides (AMPs) secreted by amphibian skin represent an important innate immune defense strategy. There are more than 340 species in the family of Ranidae worldwidely, and from which nearly 100 families of AMPs comprising between 8 and 48 amino acid (aa) residues have been characterized. In current work, two novel AMPs were purified from the skin secretion of Hainan cascade-frog, Amolops hainanensis, and 31 cDNA sequences encoding 10 novel AMPs belonging to 4 families were cloned from the constructed skin cDNA library of A. hainanensis. Among these 10 AMPs, 5 peptides represent the prototypes of a novel amphibian AMP family. According to the generic name of the species of origin, they were designated as hainanenin-1-5. Each of them consists of 21 aa residues with a C-terminal disulphide loop of 7 residues between Cys(15) and Cys(21). Two of them (hainanenin-1 and 5) were then synthesized and their in vitro activities were screened, including antimicrobial, hemolytic and antioxidant activities. The results showed that hainanenin-1 and 5 possessed strong and broad-spectrum antimicrobial activities against Gram-positive, Gram-negative bacteria and fungi, including a large number of clinically isolated drug-resistant pathogenic microorganisms, and slight antioxidant activity. Undesirably, hainanenin-1 and 5 exhibited strong hemolytic activity on human erythrocytes. The discovery of hainanenins and their great antimicrobial potency provides new templates for anti-infective agent design.
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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