Difference between revisions of "Part:BBa K4165005"
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===<span class='h3bb'>Sequence and Features</span>===
 
===<span class='h3bb'>Sequence and Features</span>===
 
<partinfo>BBa_K4165005 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K4165005 SequenceAndFeatures</partinfo>
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===Dry Lab Characterization===
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<p style=" font-weight: bold; font-size:14px;"> Modeling </p>
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<p><img src="https://static.igem.wiki/teams/4165/wiki/parts-registry/ab42/ab42-removebg-preview.png" style="margin-left:200px;" alt="" width="500" /></p>
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                                Figure 1. RCSB model of Amyloid Beta fragment 1-42
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<p style=" font-weight: bold; font-size:14px;"> Docking </p>
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ΔG = -44.19
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<p><img src="https://static.igem.wiki/teams/4165/wiki/parts-registry/ab42/ab-seed-lightdock.png" style="margin-left:200px;" alt="" width="500" /></p>
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                          Figure 2. Docked structure of AB 1-42 against Seed peptide
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ΔG = -60.075
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<p><img src="https://static.igem.wiki/teams/4165/wiki/parts-registry/ab42/ab-td28rev-lightdock.png" style="margin-left:200px;" alt="" width="500" /></p>
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                          Figure 2. Docked structure of AB 1-42 against TD28REV peptide
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ΔG = -52.452
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<p><img src="https://static.igem.wiki/teams/4165/wiki/parts-registry/ab42/ab-www-lightdock.png" style="margin-left:200px;" alt="" width="500" /></p>
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                          Figure 2. Docked structure of AB 1-42 against WWW peptide
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Revision as of 18:44, 10 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


Docking

ΔG = -44.19 


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


ΔG = -60.075 


                          Figure 2. Docked structure of AB 1-42 against TD28REV peptide


ΔG = -52.452 


                          Figure 2. Docked structure of AB 1-42 against WWW peptide



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.