Difference between revisions of "Part:BBa K4897007"
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| − | + | Caf1-AMP was introduced by BS_United_China_2023 as 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 net-like structure which limit the movement of P. acne.The antimicrobial peptides attached to the protein can selectively kill the bacteria by disrupting the cell mebrane. 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 [4]. At high temperature, long polymers of Caf1 dissociates 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 temperature and cool down into net-like structure after minutes. Second, the protein is safe for human cells, proved by previous research on its ability to encapsulate human dermal fibroblast cells while maintaining the cells’ lives [4]. Third, certain features could be added on Caf1 by attaching protein or peptides on the protein. This feature enable us to adopt AMP on the protein to effectively and selectively kill P. acne. Antimicrobial Peptides (AMPs) are small peptide molecules naturally exist for the immune system of animals [5]. 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 defend the skin from P. acne and prevent formation of acne vulgaris. | |
Revision as of 03:50, 6 October 2023
Caf1-AMP was introduced by BS_United_China_2023 as 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 net-like structure which limit the movement of P. acne.The antimicrobial peptides attached to the protein can selectively kill the bacteria by disrupting the cell mebrane. 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 [4]. At high temperature, long polymers of Caf1 dissociates 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 temperature and cool down into net-like structure after minutes. Second, the protein is safe for human cells, proved by previous research on its ability to encapsulate human dermal fibroblast cells while maintaining the cells’ lives [4]. Third, certain features could be added on Caf1 by attaching protein or peptides on the protein. This feature enable us to adopt AMP on the protein to effectively and selectively kill P. acne. Antimicrobial Peptides (AMPs) are small peptide molecules naturally exist for the immune system of animals [5]. 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 defend the skin from P. acne and prevent formation of acne vulgaris.