Difference between revisions of "Part:BBa K4165005"

 
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Amyloid β Protein Fragment 1-42 which results from the amyloidogenic degradation of Amyloid beta precursor and forms toxic plaques inside the brain leading to the development of Alzheimer's Disease.
 
Amyloid β Protein Fragment 1-42 which results from the amyloidogenic degradation of Amyloid beta precursor and forms toxic plaques inside the brain leading to the development of Alzheimer's Disease.
  
===Source===
 
APP amyloid beta precursor protein [Homo sapiens (human)] - Gene - NCBI. (2022)
 
  
 
===Usage and Biology===
 
===Usage and Biology===
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                         Figure 2. Docked structure of AB 1-42 against TD28REV peptide Visualized by Pymol.
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                         Figure 3. Docked structure of AB 1-42 against TD28REV peptide Visualized by Pymol.
  
  
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                           Figure 3. Docked structure of AB 1-42 against WWW peptide Visualized by Pymol.
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                           Figure 4. Docked structure of AB 1-42 against WWW peptide Visualized by Pymol.
  
  
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                   Figure 4. this figure shows the results from the transcription and translation code showing the  
+
                   Figure 5. this figure shows the results from the transcription and translation code showing the  
 
                       variation of mRNA and protein concentrations with time compared with the wet lab results.
 
                       variation of mRNA and protein concentrations with time compared with the wet lab results.
  

Latest revision as of 13:52, 13 October 2022


Amyloid β Protein Fragment 1-42 (Aβ 1-42)

Amyloid β Protein Fragment 1-42 which results from the amyloidogenic degradation of Amyloid beta precursor and forms toxic plaques inside the brain leading to the development of Alzheimer's Disease.


Usage and Biology

A𝛽-42 formation is due to the amyloidogenic degradation of Amyloid Precursor Protein (APP). APP is a normal cell surface receptor whose cleavage results in different types of peptides depending on the method, and those peptides serve different functions. In the amyloidogenic pathway, APP is partially cleaved by two enzymes, the first one is 𝛽-secretase which cleaves APP into 𝛽-APP and the second enzyme is 𝛾-secretase responsible for the cleavage of the remaining part of APP to form A𝛽-42 fragments. The 42 amino acid fragments are toxic in nature and form A𝛽 plaques when aggregated together. The plaques block the transmission of electrical impulses and communication between neurons, therefore causing memory loss.

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


Dry Lab Characterization

Modeling


                            Figure 1. RCSB model of Amyloid Beta fragment 1-42 visualized by Pymol.


Docking

ΔG = -44.19


                          Figure 2. Docked structure of AB 1-42 against Seed peptide visualized by Pymol.


ΔG = -60.075


                        Figure 3. Docked structure of AB 1-42 against TD28REV peptide Visualized by Pymol.


ΔG = -52.452


                         Figure 4. Docked structure of AB 1-42 against WWW peptide Visualized by Pymol.


Mathematical modeling

Transcription rate and translation rate under T7 promotor

the mathematical modeling was based on our code for the calculation of transcription and translation (you can find it in the code section) beside with the estimated results from the wet lab.



                  Figure 5. this figure shows the results from the transcription and translation code showing the 
                     variation of mRNA and protein concentrations with time compared with the wet lab results.


References

1. APP amyloid beta precursor protein [Homo sapiens (human)] - Gene - NCBI. (2022), from https://www.ncbi.nlm.nih.gov/gene/351

2. Bachurin, S. O., Bovina, E. V., & Ustyugov, A. A. (2017). Drugs in clinical trials for Alzheimer's disease: the major trends. Medicinal research reviews, 37(5), 1186-1225.

3. Carrillo-Mora, P., Luna, R., & Colín-Barenque, L. (2014). Amyloid beta: multiple mechanisms of toxicity and only some protective effects?. Oxidative medicine and cellular longevity, 2014.