AcrAP1 – Antimicrobial Peptides – AMP

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.

 

Technical specification

 KD20 peptide Sequence : H-FLFSLIPHAISGLISAFK-OH
 KD20 peptide MW : 1.961.35 g/mol
 KD20 peptide Purity : > 95%
 KD20 peptide Counter-Ion : TFA Salts
Peptide library synthesis KD20 peptide Delivery format : Lyophilized

Price

 

Product Size Price €
Price $
CRB1000028-0.5 mg 0.5 mg 141 € 113 $
CRB1000028-1 mg 1 mg 193 € 154 $
CRB1000028-
CRB1000028-
CRB1000028-

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