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Boateng, J., Matthews, K.H., Stevens, H.N.E., Eccleston, G.M., 2008. Wound Healing Dressings and Drug Delivery Systems: A Review. J. Pharm. Sci. 97. doi:10.1002/jps21210 | Boateng, J., Matthews, K.H., Stevens, H.N.E., Eccleston, G.M., 2008. Wound Healing Dressings and Drug Delivery Systems: A Review. J. Pharm. Sci. 97. doi:10.1002/jps21210 | ||
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Rnjak-Kovacina, J., Daamen, W.F., Pierna, M., Rodríguez-Cabello, J.C., Weiss, A.S., 2011. Elastin Biopolymers. Compr. Biomater. 329–346. doi:http://dx.doi.org/10.1016/B978-0-08-055294-1.00071-4 | Rnjak-Kovacina, J., Daamen, W.F., Pierna, M., Rodríguez-Cabello, J.C., Weiss, A.S., 2011. Elastin Biopolymers. Compr. Biomater. 329–346. doi:http://dx.doi.org/10.1016/B978-0-08-055294-1.00071-4 | ||
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Revision as of 09:02, 20 September 2017
Fusing
Short summary
As proof of concept, we work on enhanced stability of a protein polymer. This networks can be applied for different applications like modern biomaterials in medicine and industry (Rnjak-Kovacina et al., 2011). The amino acids Nε‑L‑cysteinyl‑L‑lysine (CL) and Nγ‑2‑cyanobenzothiazol‑6‑yl‑L‑asparagine (CBT-Asp) comprise key parts of this tool. Both amino acids can bind specificly to each other resulting in the formation of a covalent bond between their side chains. We plan to use this covalent bond to increase the stability of silk elastin like proteins (SELPs). The strengthened polymer network would be a perfect material to produce biological wound bindings which are very thin and they would be able to interact with the natural tissue matrix (Boateng et al., 2008).
Terminus independent fusion proteins
Figure 1: Reaction of the 1,2‑aminothiol of cysteine and CBT to luciferin (Liang et al., 2010).
Figure 2: Specific binding reaction of CL and CBT‑Asp.
Nε-L-cysteinyl-L-lysine
- Name: Nε-L-cysteinyl-L-lysine
- Short: CL
- Molecular Weight: 249.33 g mol-1
- Storage: -20 – 4 °C
- Function: Terminus independent binding system
Figure 3: Structure of CL.
Nγ‑2‑cyanobenzothiazol‑6‑yl‑L‑asparagine
Figure 4: Structure of CBT‑Asp.
- Name: Nγ‑2‑cyanobenzothiazol‑6‑yl‑L‑asparagine
- Short: CBT-Asp
- Molecular Weight: 290.30 g mol-1
- Storage: -20 – 4 °C
- Function: Terminus independent binding system
Silk Elastin like Proteins
Figure 5: Schematic structure of a SELP polymer network.
Silk consensus sequences are shown in green,
elastin consensus sequences are red and the blue lines show the hydrogen bonds of the consensus sequences.
Figure 6: Schematic sequence of the SELP (Collins et al., 2013).
Silk consensus sequences
are green and elastin consensus sequences are red.
Figure 7: Schematic structure of a SELP polymer network.
PRe-RDL
Figure 8: Scheme of the PRe-RDL (McDaniel et al., 2010).
References
Collins, T., Azevedo-silva, J., Costa, A., Branca, F., Machado, R., Casal, M., 2013. Batch production of a silk-elastin-like protein in E . coli BL21 ( DE3 ): key parameters for optimisation. Microb. Cell Fact. 12, 1–16. doi:10.1186/1475-2859-12-21
Liang, G., Ren, H., Rao, J., 2010. A biocompatible condensation reaction for controlled assembly of nanostructures in living cells. Nat. Chem. 2, 54–60. doi:10.1038/nchem.480
McDaniel, J.R., Mackay, J.A., Quiroz, F.G., Chilkoti, A., 2010. Recursive Directional Ligation by Plasmid Reconstruction allows Rapid and Seamless Cloning of Oligomeric Genes 11, 944–952. doi:10.1021/bm901387t.Recursive
Nguyen, D.P., Elliott, T., Holt, M., Muir, T.W., Chin, J.W., 2011. Genetically Encoded 1,2-Aminothiols Facilitate Rapid and Site-Specific Protein Labeling via a Bio-orthogonal Cyanobenzothiazole Condensation. J. Am. Chem. Soc. 133, 11418–11421. doi:10.1021/ja203111c
Rnjak-Kovacina, J., Daamen, W.F., Pierna, M., Rodríguez-Cabello, J.C., Weiss, A.S., 2011. Elastin Biopolymers. Compr. Biomater. 329–346. doi:http://dx.doi.org/10.1016/B978-0-08-055294-1.00071-4