Translational_Unit

Part:BBa_K2278022

Designed by: Paul ZANONI   Group: iGEM17_INSA-UPS_France   (2017-10-08)
Revision as of 17:49, 8 October 2017 by Pzanoni (Talk | contribs)

Lecrocin I AMP with alpha-factor secretion signal

Introduction

Antimicrobial peptides are phygenitically ancient components of innate defense mechanisms of both invertebrates and vertebrates. In the context of growing prevalence of antibiotic-resistance of bacterial strain, the AMP can be considered as potential new therapeutical candidates. Leucrocin I from Siamese crocodile white blood cells shows a good antibacterial activity towards Vibrio cholerae. The peptide is a 7 amino acid residue : NGVQPKY with a molecular mass around 806.99 Da. The mechanism of action of the Leucrocin I has been observed with fluorescence and electron microscopy This cationic molecules and can target bacterium membranes, to create pores in it, leading to the lysis of the cells. The part was designed to constitutively produce the leucrocin I AMP with a yeast promoter. The α-factor sequence contains a RBS and a signal sequence to secrete the produced peptides. The pGAP promoter is used because it makes genome recombination easier in Pichia pastoris genome. The restriction enzyme sites are set up to extract individually each components of the plasmid. It belongs to the respond module in the Croc’n cholera project of iGEM INSA-UPS-France 2017

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