Difference between revisions of "Part:BBa K4897008"
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<partinfo>BBa_K4897008 short</partinfo> | <partinfo>BBa_K4897008 short</partinfo> | ||
− | Here we use | + | Here we use GPX7 expression system(BBa_K4897006) and Caf1-AMP(BBa_K4897007) assembly system to generate the key component of BS cleanser. |
− | Glutathione peroxidase7 (GPX 7) is | + | Glutathione peroxidase7 (GPX 7) is an antioxidant enzyme in mammals in response to oxidative stress [1]. Oxidative stress essentially causes the aging of the skin and is typically caused by reactive oxygen species [2]. One of the reactive oxygen species that appear commonly on the human face is hydrogen peroxide. However, GPX7 can catalyze the reaction to reduce hydrogen peroxide to water and prevent the oxidation and aging of the skin [2],[3]. This is a way to nourish the skin in addition to the prevention of acne. |
We developed the new part of TurboID-SP based on the TurboID part design of last year’s BS_United_China 2022 [6]. TurboID-SP is a protein ligase that binds biotin in around 10 minutes [7]. Through the binding of TurboID to a specific protein’s signal peptide that belongs to P. acne, biotinylation occurs to bind biotin onto a protein (specifically its lysine residues). Alongside streptavidin-phycoerythrin [8], we successfully inhibit the quorum sensing mechanism of bacteria. When TurboID binds to the signal peptides of a protein, ATP and biotin are catalyzed together to produce biotinyl-5'-AMP. Using the energy from ATP, the product of biotnyl-5'-AMP can label selected proteins. The biotin bound to the protein then accumulates and effectively blocks the receptors of bacteria P. acne. Streptavidin-phycoerythrin can also join the biotin, creating an even larger barrier that blocks receptors and enabling a double-blocking system for quorum sensing. Consequently, it will be difficult for P. acne to communicate and undergo normal functions, such as virulence factor production and pathogenic behaviors [9]. | We developed the new part of TurboID-SP based on the TurboID part design of last year’s BS_United_China 2022 [6]. TurboID-SP is a protein ligase that binds biotin in around 10 minutes [7]. Through the binding of TurboID to a specific protein’s signal peptide that belongs to P. acne, biotinylation occurs to bind biotin onto a protein (specifically its lysine residues). Alongside streptavidin-phycoerythrin [8], we successfully inhibit the quorum sensing mechanism of bacteria. When TurboID binds to the signal peptides of a protein, ATP and biotin are catalyzed together to produce biotinyl-5'-AMP. Using the energy from ATP, the product of biotnyl-5'-AMP can label selected proteins. The biotin bound to the protein then accumulates and effectively blocks the receptors of bacteria P. acne. Streptavidin-phycoerythrin can also join the biotin, creating an even larger barrier that blocks receptors and enabling a double-blocking system for quorum sensing. Consequently, it will be difficult for P. acne to communicate and undergo normal functions, such as virulence factor production and pathogenic behaviors [9]. | ||
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<partinfo>BBa_K4897008 parameters</partinfo> | <partinfo>BBa_K4897008 parameters</partinfo> | ||
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+ | ===References=== | ||
+ | [1]GPX7 glutathione peroxidase 7 [Homo sapiens (human)] - Gene - NCBI. (n.d.). Retrieved from www.ncbi.nlm.nih.gov website: https://www.ncbi.nlm.nih.gov/gene/2882 | ||
+ | <br> | ||
+ | [2]Rinnerthaler, M., Bischof, J., Streubel, M., Trost, A., & Richter, K. (2015). Oxidative Stress in Aging Human Skin. Biomolecules, 5(2), 545–589. https://doi.org/10.3390/biom5020545 | ||
+ | <br> | ||
+ | [3]UniProt. (n.d.). Retrieved October 4, 2023, from www.uniprot.org website: https://www.uniprot.org/uniprotkb/Q96SL4/entry | ||
+ | <br> |
Revision as of 11:14, 8 October 2023
GPX7, Caf1-AMP, and TurboID-FGB for Eliminating P. acne
Here we use GPX7 expression system(BBa_K4897006) and Caf1-AMP(BBa_K4897007) assembly system to generate the key component of BS cleanser.
Glutathione peroxidase7 (GPX 7) is an antioxidant enzyme in mammals in response to oxidative stress [1]. Oxidative stress essentially causes the aging of the skin and is typically caused by reactive oxygen species [2]. One of the reactive oxygen species that appear commonly on the human face is hydrogen peroxide. However, GPX7 can catalyze the reaction to reduce hydrogen peroxide to water and prevent the oxidation and aging of the skin [2],[3]. This is a way to nourish the skin in addition to the prevention of acne.
We developed the new part of TurboID-SP based on the TurboID part design of last year’s BS_United_China 2022 [6]. TurboID-SP is a protein ligase that binds biotin in around 10 minutes [7]. Through the binding of TurboID to a specific protein’s signal peptide that belongs to P. acne, biotinylation occurs to bind biotin onto a protein (specifically its lysine residues). Alongside streptavidin-phycoerythrin [8], we successfully inhibit the quorum sensing mechanism of bacteria. When TurboID binds to the signal peptides of a protein, ATP and biotin are catalyzed together to produce biotinyl-5'-AMP. Using the energy from ATP, the product of biotnyl-5'-AMP can label selected proteins. The biotin bound to the protein then accumulates and effectively blocks the receptors of bacteria P. acne. Streptavidin-phycoerythrin can also join the biotin, creating an even larger barrier that blocks receptors and enabling a double-blocking system for quorum sensing. Consequently, it will be difficult for P. acne to communicate and undergo normal functions, such as virulence factor production and pathogenic behaviors [9].
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]
References
[1]GPX7 glutathione peroxidase 7 [Homo sapiens (human)] - Gene - NCBI. (n.d.). Retrieved from www.ncbi.nlm.nih.gov website: https://www.ncbi.nlm.nih.gov/gene/2882
[2]Rinnerthaler, M., Bischof, J., Streubel, M., Trost, A., & Richter, K. (2015). Oxidative Stress in Aging Human Skin. Biomolecules, 5(2), 545–589. https://doi.org/10.3390/biom5020545
[3]UniProt. (n.d.). Retrieved October 4, 2023, from www.uniprot.org website: https://www.uniprot.org/uniprotkb/Q96SL4/entry