Difference between revisions of "Part:BBa K4897007"

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===What is it?===
 
===What is it?===
  
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Caf1-AMP is a protein to captures and suppresses P. acne, our identified main pathogen for acne formation. In short, Caf1-AMP, after entering the pores on human faces at a relatively warm temperature, can cool down to repolymerize into a net-like structure which limits the movement of P. acne. The antimicrobial peptides attached to the protein can selectively kill the bacteria by disrupting the cell membrane. This synthetic protein contains two parts: Capsular antigen fragment 1 (Caf1) and Antimicrobial Peptides (AMPs). Caf1 is a bacterial protein that possesses three valuable features that benefit our project. First, it is a unique protein that is thermally reformable [1]. At high temperature, long polymers of Caf1 dissociate into subunits; at low temperature, the subunits reforms into polymers without losing their function. This feature allows the protein to enter tiny pores on human faces at warm temperatures and cool down into a net-like structure after minutes. Second, the protein is safe for human cells, as proved by previous research on its ability to encapsulate human dermal fibroblast cells while maintaining the cells’ lives [1]. Third, certain features could be added to Caf1 by attaching protein or peptides to the protein. This feature enables us to adopt AMP on the protein to effectively and selectively kill P. acne. Antimicrobial Peptides (AMPs) are small peptide molecules that naturally exist for the immune system of animals [2]. In general, it adopts a broad range of mechanisms to defend the host against a variety of pathogens including bacteria. Through research, we found effective AMP that is selectively harmful for P. acne and use it in our synthetic protein. Overall, Caf1-AMP serves an important role in defending the skin from P. acne and preventing the formation of acne vulgaris.
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Caf1-AMP is a protein to capture and suppress P. acne, our identified main pathogen for acne formation. In short, Caf1-AMP, after entering the pores on human faces at a relatively warm temperature, can cool down to repolymerize into a net-like structure which limits the movement of P. acne. The antimicrobial peptides attached to the protein can selectively kill the bacteria by disrupting the cell membrane. This synthetic protein contains two parts: Capsular antigen fragment 1 (Caf1) and Antimicrobial Peptides (AMPs). Caf1 is a bacterial protein that possesses three valuable features that benefit our project. First, it is a unique protein that is thermally reformable [1]. At high temperature, long polymers of Caf1 dissociate into subunits; at low temperature, the subunits reforms into polymers without losing their function. This feature allows the protein to enter tiny pores on human faces at warm temperatures and cool down into a net-like structure after minutes. Second, the protein is safe for human cells, as proved by previous research on its ability to encapsulate human dermal fibroblast cells while maintaining the cells’ lives [1]. Third, certain features could be added to Caf1 by attaching protein or peptides to the protein. This feature enables us to adopt AMP on the protein to effectively and selectively kill P. acne. Antimicrobial Peptides (AMPs) are small peptide molecules that naturally exist for the immune system of animals [2]. In general, it adopts a broad range of mechanisms to defend the host against a variety of pathogens including bacteria. Through research, we found effective AMP that is selectively harmful for P. acne and use it in our synthetic protein. Overall, Caf1-AMP serves an important role in defending the skin from P. acne and preventing the formation of acne vulgaris.
  
 
===Usage and Biology===
 
===Usage and Biology===
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<table width="100%" border="10" cellspacing="0" cellpadding="0">
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  <tr>
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    <td align="center"><img src="https://static.igem.wiki/teams/4897/wiki/parts/caf1-amp-biology-demonstration.png" width="800" height="auto" /> </td>
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  </tr>
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    <td align="center">Fig. 1. The composition and structure of Caf1-AMP</td>
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  </tr>
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</table>
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</html>
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Caf1-AMP is used to capture and suppress P. acne on human skin. While the Caf1 subunit of this part can limit the movement, specifically escape, of P. acne, the AMP subunit is able to damage the cell membrane of P. acne. Furthermore, AMP is effective for many pathogens, not only P. acne. Thus, Caf-AMP can be technically used to suppress other bacteria, but this is not recommended.
 
Caf1-AMP is used to capture and suppress P. acne on human skin. While the Caf1 subunit of this part can limit the movement, specifically escape, of P. acne, the AMP subunit is able to damage the cell membrane of P. acne. Furthermore, AMP is effective for many pathogens, not only P. acne. Thus, Caf-AMP can be technically used to suppress other bacteria, but this is not recommended.
  
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Lane M is the Marker, and all other lanes are repeated results of Caf-AMP at 30 Celsius Degrees.
 
Lane M is the Marker, and all other lanes are repeated results of Caf-AMP at 30 Celsius Degrees.
 
Since a Caf1 monomer has a mass of around 15 kDa [1], and the mass of the small AMP peptide is negligible, the identification result in the graph is correct, demonstrating the 15 kDa monomer.
 
Since a Caf1 monomer has a mass of around 15 kDa [1], and the mass of the small AMP peptide is negligible, the identification result in the graph is correct, demonstrating the 15 kDa monomer.
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<span class='h3bb'>Sequence and Features</span>
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<partinfo>BBa_K4897007 SequenceAndFeatures</partinfo>
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===Functional Parameters===
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<partinfo>BBa_K4897007 parameters</partinfo>
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===References===
 
===References===
 
[1]Dura, G., Peters, D. L., Waller, H. L., Yemm, A. I., Perkins, N. J., Ferreira, A., … Fulton, D. (2020). A Thermally Reformable Protein Polymer. 6(11), 3132–3151. https://doi.org/10.1016/j.chempr.2020.09.020
 
[1]Dura, G., Peters, D. L., Waller, H. L., Yemm, A. I., Perkins, N. J., Ferreira, A., … Fulton, D. (2020). A Thermally Reformable Protein Polymer. 6(11), 3132–3151. https://doi.org/10.1016/j.chempr.2020.09.020
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<br>
 
[2]Zhang, Q.-Y., Yan, Z.-B., Meng, Y.-M., Hong, X.-Y., Shao, G., Ma, J.-J., … Fu, C.-Y. (2021). Antimicrobial peptides: mechanism of action, activity and clinical potential. Military Medical Research, 8, 48. https://doi.org/10.1186/s40779-021-00343-2.
 
[2]Zhang, Q.-Y., Yan, Z.-B., Meng, Y.-M., Hong, X.-Y., Shao, G., Ma, J.-J., … Fu, C.-Y. (2021). Antimicrobial peptides: mechanism of action, activity and clinical potential. Military Medical Research, 8, 48. https://doi.org/10.1186/s40779-021-00343-2.

Latest revision as of 00:20, 10 October 2023

Capsular antigen fragment 1-Antimicrobial Peptides

What is it?

Caf1-AMP is a protein to capture and suppress P. acne, our identified main pathogen for acne formation. In short, Caf1-AMP, after entering the pores on human faces at a relatively warm temperature, can cool down to repolymerize into a net-like structure which limits the movement of P. acne. The antimicrobial peptides attached to the protein can selectively kill the bacteria by disrupting the cell membrane. This synthetic protein contains two parts: Capsular antigen fragment 1 (Caf1) and Antimicrobial Peptides (AMPs). Caf1 is a bacterial protein that possesses three valuable features that benefit our project. First, it is a unique protein that is thermally reformable [1]. At high temperature, long polymers of Caf1 dissociate into subunits; at low temperature, the subunits reforms into polymers without losing their function. This feature allows the protein to enter tiny pores on human faces at warm temperatures and cool down into a net-like structure after minutes. Second, the protein is safe for human cells, as proved by previous research on its ability to encapsulate human dermal fibroblast cells while maintaining the cells’ lives [1]. Third, certain features could be added to Caf1 by attaching protein or peptides to the protein. This feature enables us to adopt AMP on the protein to effectively and selectively kill P. acne. Antimicrobial Peptides (AMPs) are small peptide molecules that naturally exist for the immune system of animals [2]. In general, it adopts a broad range of mechanisms to defend the host against a variety of pathogens including bacteria. Through research, we found effective AMP that is selectively harmful for P. acne and use it in our synthetic protein. Overall, Caf1-AMP serves an important role in defending the skin from P. acne and preventing the formation of acne vulgaris.

Usage and Biology

Fig. 1. The composition and structure of Caf1-AMP

Caf1-AMP is used to capture and suppress P. acne on human skin. While the Caf1 subunit of this part can limit the movement, specifically escape, of P. acne, the AMP subunit is able to damage the cell membrane of P. acne. Furthermore, AMP is effective for many pathogens, not only P. acne. Thus, Caf-AMP can be technically used to suppress other bacteria, but this is not recommended.

Characterization

Fig. 2. Characterization of Caf1-AMP using Western Blotting
Lane M is the Marker, and all other lanes are repeated results of Caf-AMP at 30 Celsius Degrees. Since a Caf1 monomer has a mass of around 15 kDa [1], and the mass of the small AMP peptide is negligible, the identification result in the graph is correct, demonstrating the 15 kDa monomer.

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]


References

[1]Dura, G., Peters, D. L., Waller, H. L., Yemm, A. I., Perkins, N. J., Ferreira, A., … Fulton, D. (2020). A Thermally Reformable Protein Polymer. 6(11), 3132–3151. https://doi.org/10.1016/j.chempr.2020.09.020
[2]Zhang, Q.-Y., Yan, Z.-B., Meng, Y.-M., Hong, X.-Y., Shao, G., Ma, J.-J., … Fu, C.-Y. (2021). Antimicrobial peptides: mechanism of action, activity and clinical potential. Military Medical Research, 8, 48. https://doi.org/10.1186/s40779-021-00343-2.