RBS - Antifungal D4E1 - Double terminator
D4E1 is a synthetic peptide, a linear analogue of Cecropin B AMPs (antimicrobial peptides), and has antibacterial and antifungal properties. D4E1 is composed of seventeen amino acids, and has a beta sheet conformation in solution. Lethality of D4E1 appears to be due to the peptide binding to sterols present in the fungal conidial surface, thus inhibiting the spore germination. It has also been shown that D4E1 has resistance to fungal and plant protease degradation.
Sequence and Features
This part is composed of a RBS (K780002 strong RBS), the open reading frame of D4E1 and a double terminator (B0015). This part was optimized for its expression and its secretion in Bacillus subtilis. The coding sequence of D4E1 was flanked on the N-terminal end with a signal peptide (amyE signal peptide) followed by a pro peptide, cleaved during the secretion process.
To see the characterization of this biobrick, please go to K1364009.
- 10COMPATIBLE WITH RFC
- 12COMPATIBLE WITH RFC
- 21COMPATIBLE WITH RFC
- 23COMPATIBLE WITH RFC
- 25Illegal NgoMIV site found at 59
- 1000COMPATIBLE WITH RFC
Kanniah Rajasekaran, Kurt D. Stromberg, Jeffrey W. Cary, and Thomas E. Cleveland. Broad- Spectrum Antimicrobial Activity in vitro of the Synthetic Peptide D4E1. J. Agric. Food Chem. 2001, Vol. 49, 2799-2803.
A.J De Lucca, J.M Bland, C. Grimm, T.J Jacks. Fungicidal properties, sterol binding, and proteolytic resistance of the synthetic peptide D4E1. Canadian Journal of Microbiology. 1998, Vol. 44:514-520.