• Description

  • Application Data


An antimicrobial peptide (AMP) from the venom of Androctonus crassicauda.

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Application Data

Catalogue number crb1000028
Molecular Weight 1961.35
Sequence (one letter code)


Sequence (three letter code)


Purity >95%
Storage - 20 ° C

Calvete et al., (2017). Venomics: integrative venom proteomics and beyond. Biochem. J. 474(5): 611.


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 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 as 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.


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