An antimicrobial peptide (AMP) from the venom of Androctonus crassicauda.
Catalogue number crb1000028 Molecular Weight 1961.35 Sequence (one letter code) FLFSLIPHAISGLISAFK-acid Sequence (three letter code) H-Phe-Leu-Phe-Ser-Leu-Ile-Pro-His-Ala-Ile-Ser-Gly-Leu-Ile-Ser-Ala-Phe-Lys-OH Molecular Weight 1961.35 Purity >95% Storage - 20 ° C References Qiang Du et al. Int J Biol Sci 2014; 10(10):1097-1107
Venom peptidomes and proteomes have yielded significant novel drug discoveries. The non-disulphide bridge peptides (NDBPs) have become a particular focus due to their large range of structures as well biological activity while retaining high specificity.
In scorpion venom A. crassicauda, AcrAP1 was identified as a NDBP. Data shows it has antimicrobial activity against bacteria and yeast while also capable of haemolysing of horse erythrocytes. However, AcrAP1 did not affect the growth of the cancerous cell lines tested. Therefore, this peptide could be a useful model for modification to improve its potency. Furthermore, it may allow researchers to identify specific targets in disease pathways for new drug designs. A significant example of this, bradykinin-potentiating peptide Captopril® manages hypertension and originated from the conserved NDBP family.