Part:BBa_K2959001
Expressible LL 37 with Arabinose Inducible Promoter
This composite part enables tha expression of the human antimicrobial peptide LL 37. The BioBrick consists of parts araC-pBad-rbs-LL37 (BBa_K1230007) and a doulbe terminator (BBa_B0015). The part was designed with the purpose of expressing the peptide in E. coli. Expression of the part is regulated by the pBAD promoter which is inducible through arabinose. The promoter was designed to have low background activty which is ideal for porduction of toxic peptides which is the case of LL 37 production in E. coli. Also, we added part BBa_B0015 in order to create a ready-to-express version of part BBa_K1230007.
Usage and Biology
The protein LL-37 cathelicidin is a human antimicrobial peptide active against Gram-positive bacteria, Gram-negative bacteria and fungi1. LL-37 is the only known cathelicidin peptide produced in humans; its structure is amphipathic and has an α-helical conformation with a positive charge. Talking about its mechanism of action, the cathelicidins targeted the cell membrane and causes its complete disruption inducing cell membrane permeabilization and simultaneous vacuolar expansion. Intracellular activities of the peptide may contribute to its antifungal activity2.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BamHI site found at 1144
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 979
- 1000INCOMPATIBLE WITH RFC[1000]Illegal SapI site found at 961
References
1. Tollin, M. & Bergman, P. (2003). Antimicrobial peptides in the first line defence of human colon mucosa. (4):523-30 DOI:10.1016/s0196-9781(03)00114-1
2. Ordonez, S. R., Amarullah, I. H., Wubbolts, R. W., Veldhuizen, E. J., & Haagsman, H. P. (2014). Fungicidal mechanisms of cathelicidins LL-37 and CATH-2 revealed by live-cell imaging. Antimicrobial agents and chemotherapy, 58(4), 2240-2248. DOI: 10.1128/AAC.01670-13
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