Difference between revisions of "Part:BBa K3351007"
 
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<partinfo>BBa_K3351007 short</partinfo>
 
<partinfo>BBa_K3351007 short</partinfo>
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===Summary===
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P6.2 is typical linear cation α-helical peptide.<br>
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Destroy the biomass membrane:<br>
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1. The combination of cationic peptide and anionic plasma membrane caused by electrostatic interaction.<br>
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2. AMP transforms from random coils to amphiphilic α helix, making Trp arranged on the same side of α helix; because of the hydrophobicity of AMP, Trp residues can be inserted into the carbon chain region of the membrane more easily, and AMP is arranged parallel to the membrane  , With the accumulation of AMP binding, the outer layer of the bilayer lipid molecule layer expands and becomes thinner, destroying the plasma membrane.<br>
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Due to the cationic nature of P5 and P6.2, they can be inserted between negatively charged bacterial cells, interfere with the interaction of extracellular polymers (EPS), and reduce EPS accumulation.<br>
  
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P6.2 is typical linear cation α-helical peptide.
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===Characterization===
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Destroy the biomass membrane:
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1. The combination of cationic peptide and anionic plasma membrane caused by electrostatic interaction.
+
−
2. AMP transforms from random coils to amphiphilic α helix, making Trp arranged on the same side of α helix; because of the hydrophobicity of AMP, Trp residues can be inserted into the carbon chain region of the membrane more easily, and AMP is arranged parallel to the membrane  , With the accumulation of AMP binding, the outer layer of the bilayer lipid molecule layer expands and becomes thinner, destroying the plasma membrane.
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−
Due to the cationic nature of P5 and P6.2, they can be inserted between negatively charged bacterial cells, interfere with the interaction of extracellular polymers (EPS), and reduce EPS accumulation.
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<html>
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<img style="display: block;
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    width: 60%;height: 60%;" src="https://static.igem.org/mediawiki/parts/b/bc/T--NWU-CHINA-A--od-5.png"><div>Figure.1 growth curve</div></html>
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===Reference===
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[1] Martínez M, Polizzotto A, Flores N, Semorile L, Maffía PC. Antibacterial, anti-biofilm and in vivo activities of the antimicrobial peptides P5 and P6.2. Microb Pathog. 2020 Feb;139:103886. doi: 10.1016/j.micpath.2019.103886. Epub 2019 Nov 25. PMID: 31778756.
 
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===Usage and Biology===
 
===Usage and Biology===

Latest revision as of 10:42, 26 October 2020


P6.2, an antimicrobial peptide.

Summary

P6.2 is typical linear cation α-helical peptide.
Destroy the biomass membrane:
1. The combination of cationic peptide and anionic plasma membrane caused by electrostatic interaction.
2. AMP transforms from random coils to amphiphilic α helix, making Trp arranged on the same side of α helix; because of the hydrophobicity of AMP, Trp residues can be inserted into the carbon chain region of the membrane more easily, and AMP is arranged parallel to the membrane , With the accumulation of AMP binding, the outer layer of the bilayer lipid molecule layer expands and becomes thinner, destroying the plasma membrane.
Due to the cationic nature of P5 and P6.2, they can be inserted between negatively charged bacterial cells, interfere with the interaction of extracellular polymers (EPS), and reduce EPS accumulation.

Characterization

Figure.1 growth curve

Reference

[1] Martínez M, Polizzotto A, Flores N, Semorile L, Maffía PC. Antibacterial, anti-biofilm and in vivo activities of the antimicrobial peptides P5 and P6.2. Microb Pathog. 2020 Feb;139:103886. doi: 10.1016/j.micpath.2019.103886. Epub 2019 Nov 25. PMID: 31778756. 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]