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Over-expression of antimicrobial, anticancer and transmembrane peptides in Escherichia coli through a calmodulin-peptide fusion system.

J Am Chem Soc.. 2016-09; 
Vogel,Hans J.Aizawa, Tomoyasu Gopal, Ramamourthy Nguyen, Leonard T. Ishida, Hiroaki
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Peptide Synthesis ... This CaM was expressed and purified from E. coli BL21(DE3) as described previously. 53 The peptides used here were purchased as synthetic peptides with >95 % purity from Genscript (San Diego, CA). Page 10 of 30 ACS Paragon Plus Environment ... Get A Quote

摘要

The article studies calmodulin (CaM) as a more universal carrier protein to express many types of AMPs in Escherichia coli. It demonstrates the expression of various antimicrobial peptides (AMPs) using a CaM-fusion expression system, including melittin, fowlicidin-1, tritrpticin, indolicidin, puroindoline A peptide, magainin II F5W, lactoferrampin B, MIP3alpha51-70, and human beta-defensin 3 (HBD-3), the latter requiring three disulfide bonds for proper folding. It proposes the use of the CaM-fusion system as a universal approach to express many cationic amphipathic peptides.

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