AcrAP2a FLFKLIPKAIKGLLKAFK-acid

  • Description

  • Application Data

Description

AcrAP2a is cationicity-enhanced analogue of AcrAP2 (from the venom of the scorpion Androctonus crassicauda). AcrAP2a exhibited a broader spectrum of activity as well as increased potency.

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Application Data

Catalogue number crb1000031
Molecular Weight 2075.67
Sequence (one letter code) FLFKLIPKAIKGLLKAFK-acid
Sequence (three letter code)

H-Phe-Leu-Phe-Ser-Leu-Ile-Pro-Lys-Ala-Ile-Lys-Gly-Leu-Leu-Lys-Ala-Phe-Lys-OH

Purity >95%
Storage - 20 ° C
References

Calvete et al., (2017). Venomics: integrative venom proteomics and beyond. Biochem. J. 474(5): 611. https://doi.org/10.1042/BCJ20160577.

 

Qiang Du et al., (2014). Cationicity-enhanced analogues of the antimicrobial peptides, AcrAP1 and AcrAP2, from the venom of the scorpion, Androctonus crassicauda, display potent growth modulation effects on human cancer cell lines.  Int. J. Biol. Sci. 10(10):1097. PMID: 25332684.

Manufactured in: United Kingdom
Data Sheet Material Safety Data Sheet (MSDS)

Venom peptidomes and proteomes have the potential for significant inroads to novel drug discovery. The non-disulphide bridge peptides (NDBPs) have become a particular focus due to their large range of apparent structures as well biological activity while retaining high specificity.

Within the peptidome AcrAP2 was identified in the NDBP as having antimicrobial and bactericidal activity. The nascent peptide contains a predicted hydrophobic region, this was altered to lysine residues generating a hydrophilic region, AcrAP1a. This cationic enhancement markedly increases their antibacterial potency against bacteria and yeast. Furthermore, at all concentrations it inhibited proliferation of the cancer cell lines tested. The duality of AcrAP2a on growth modulation in cancer cell lines as well as having potent antimicrobial activity suggests it is a useful analogue for further research in bacteria and eukaryotes.

AcrAP2a

Cat No.Pack SizePriceQty.
1mg£110.00
0.5mg£85.00
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