Part:BBa_K3139013:Design
Optimized anti-plasmodium fusion protein
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 409
- 1000COMPATIBLE WITH RFC[1000]
Design Notes
With TEV protease recognition and cleavage sites added between each 2 peptide coding domains, the fusion protein could be cleaved with TEV protease and each peptide effects separately. And with this design, the function of our fusion protein could be more easily stimulated than using a complete fusion one (with no or part cleavage), since we got the effects of each single peptide but not the fusion one.
Source
The source of this part has been described in each page of the basic parts consisted.
References
[1] Gao B, Rodriguez M D, Lanzmendoza H, et al. AdDLP, a bacterial defensin-like peptide, exhibits anti-Plasmodium activity[J]. Biochem Biophys Res Commun, 2009, 387(2):393-398. [2] Possani L D, Zurita M, Delepierre M, et al. From noxiustoxin to Shiva-3, a peptide toxic to the sporogonic development of Plasmodium berghei.[J]. Toxicon, 1998, 36(11):1683-1692. [3] Ghosh A K, Ribolla P E M, Jacobs-Lorena M. Targeting Plasmodium ligands on mosquito salivary glands and midgut with a phage display peptide library[J]. Proceedings of the National Academy of Sciences of the United States of America, 2001, 98(23):13278-13281. [4] Moreira C K, Rodrigues F G, Ghosh A, et al. Effect of the antimicrobial peptide gomesin against different life stages of Plasmodium spp[J]. Experimental Parasitology, 2007, 116(4):346-353. [5] Tian C, Gao B, Rodriguez M C, et al. Gene expression, antiparasitic activity, and functional evolution of the drosomycin family.[J]. Molecular Immunology, 2008, 45 [6] Design and Activity of Antimicrobial Peptides against Sporogonic-Stage Parasites Causing Murine Malarias. Romanico B. G. Arrighi, Chikashi Nakamura, Jun Miyake, Hilary Hurd, J. Grant Burgess. Antimicrobial Agents and Chemotherapy Jul 2002, 46 (7) 2104-2110; DOI: 10.1128/AAC.46.7.2104-2110.2002 [7] Thiostrepton and Derivatives Exhibit Antimalarial and Gametocytocidal Activity by Dually Targeting Parasite Proteasome and Apicoplast. Makoah N. Aminake, Sebastian Schoof, Ludmilla Sologub, Monika Leubner, Marc Kirschner, Hans-Dieter Arndt, Gabriele Pradel. DOI: 10.1128/AAC.01096-10 [8] Shunyi Zhu, Bin Gao, André Aumelas, Maria del Carmen Rodríguez, Humberto Lanz-Mendoza, Steve Peigneur, Elia Diego-Garcia, Marie-France Martin-Eauclaire, Jan Tytgat, Lourival D. Possani, MeuTXKβ1, a scorpion venom-derived two-domain potassium channel toxin-like peptide with cytolytic activity, Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, Volume 1804, Issue 4, 2010, Pages 872-883, ISSN 1570-9639, https://doi.org/10.1016/j.bbapap.2009.12.017.