Difference between revisions of "Part:BBa K4165012"
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Figure 1. Docked structure of seed peptide against PHF* of fibrils | Figure 1. Docked structure of seed peptide against PHF* of fibrils | ||
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<p style=" font-weight: bold; font-size:14px;"> ΔG = -44.19 </p> | <p style=" font-weight: bold; font-size:14px;"> ΔG = -44.19 </p> |
Revision as of 18:11, 10 October 2022
Seed peptide (GGVVIA)
This part encodes Amyloid 𝛽 seed (37-42) which has the ability to bind to A𝛽 plaques inside the brain.
Usage and Biology
A short peptide derived from amyloid beta oligomers (A𝛽 37-42), which is proven to bind amyloid beta plaques inside the brain and stop plaque formation. This peptide showed no cytotoxicity when tested inside hippocampal cell lines, so it will be suitable to use as the targeting domain for A𝛽 plaques inside our system.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Dry Lab Characterization
Modeling
Figure 1. RCSB model of seed peptide (37-42)
Docking
ΔG = -168.522
Figure 1. Docked structure of seed peptide against whole tau aggregates
ΔG = -4.301
Figure 1. Docked structure of seed peptide against PHF of fibrils
ΔG = -2.769
Figure 1. Docked structure of seed peptide against PHF* of fibrils
ΔG = -44.19
Figure 1. Docked structure of seed peptide against amyloid beta
References
1. Fradinger, E. A., Monien, B. H., Urbanc, B., Lomakin, A., Tan, M., Li, H., Spring, S. M., Condron, M. M., Cruz, L., Xie, W., Benedek, G. B., & Bitan, G. (2008). C-terminal peptides coassemble into Aβ42 oligomers and protect neurons against Aβ42-induced neurotoxicity. Proceedings of the National Academy of Sciences of the United States of America, 105(37), 14175-14180. https://doi.org/10.1073/pnas.0807163105