AcrAP1a is cationicity-enhanced analogue of AcrAP1 (from the venom of the scorpion Androctonus crassicauda). AcrAP1a exhibited a broader spectrum of activity as well as increased potency.
Catalogue number crb1000030 Molecular Weight 2075.67 Sequence (one letter code) FLFKLIPKAIKGLIKAFK-acid Sequence (three letter code) H-Phe-Leu-Phe-Ser-Leu-Ile-Pro-Lys-Ala-Ile-Lys-Gly-Leu-Ile-Lys-Ala-Phe-Lys-OH Molecular Weight 2075.67 Purity >95% Storage - 20 ° C References Qiang Du et al. Int J Biol Sci 2014; 10(10):1097-1107
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 and biological activity while retaining high specificity. Additionally, it has been found that a few site-specific modifications or post-translational modifications can have significant impacts on the potency of their biological effects.
Within the peptidome AcrAP1 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 relatively high concentrations it inhibited proliferation of several cancer cell lines but at low concentrations in 2 cell lines the growth was significantly promoted. The duality of AcrAP1a 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.