Difference between revisions of "Part:BBa K1104301"
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Different from well-studied Defensins secreted from human, our Defensin1 from honey bee has many unclear properties. Even so, its effectiveness against microbes has been proved through some stable papers.</p> | Different from well-studied Defensins secreted from human, our Defensin1 from honey bee has many unclear properties. Even so, its effectiveness against microbes has been proved through some stable papers.</p> | ||
<p> Importantly, the sequence here is the mature peptide sequence because there are some introns which are barriers for ''E. coli'' to transcript genes in the genome DNA. That is to say, it is better to synthesize the gene through designing primers(about two sets >> four primers) as modules for real PCR. Comparatively, purifying genes & proteins from bees' genome DNA extraction is a more complicated and time-consuming method.</p> | <p> Importantly, the sequence here is the mature peptide sequence because there are some introns which are barriers for ''E. coli'' to transcript genes in the genome DNA. That is to say, it is better to synthesize the gene through designing primers(about two sets >> four primers) as modules for real PCR. Comparatively, purifying genes & proteins from bees' genome DNA extraction is a more complicated and time-consuming method.</p> | ||
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==''Working Mechanism(the same as normal antimicrobial peptides)''== | ==''Working Mechanism(the same as normal antimicrobial peptides)''== | ||
<p> The cytoplasmic membrane is a frequent target, but peptides may also interfere with DNA and protein synthesis, protein folding, and cell wall synthesis. The initial contact between the peptide and the target organism is electrostatic, as most bacterial surfaces are anionic, or hydrophobic. Their amino acid composition, amphipathicity, cationic charge and size allow them to attach to and insert into membrane bilayers to form pores by ‘barrel-stave’, ‘carpet’ or ‘toroidal-pore’ mechanisms. Alternately, they may penetrate into the cell to bind intracellular molecules which are crucial to cell living. Intracellular binding models includes inhibition of cell wall synthesis, alteration of the cytoplasmic membrane, activation of autolysin, inhibition of DNA, RNA, and protein synthesis, and inhibition of certain enzymes. One emerging technique for the study of such mechanisms is dual polarisation interferometry. In contrast to many conventional antibiotics these peptides appear to be bactericidal instead of bacteriostatic.</p> | <p> The cytoplasmic membrane is a frequent target, but peptides may also interfere with DNA and protein synthesis, protein folding, and cell wall synthesis. The initial contact between the peptide and the target organism is electrostatic, as most bacterial surfaces are anionic, or hydrophobic. Their amino acid composition, amphipathicity, cationic charge and size allow them to attach to and insert into membrane bilayers to form pores by ‘barrel-stave’, ‘carpet’ or ‘toroidal-pore’ mechanisms. Alternately, they may penetrate into the cell to bind intracellular molecules which are crucial to cell living. Intracellular binding models includes inhibition of cell wall synthesis, alteration of the cytoplasmic membrane, activation of autolysin, inhibition of DNA, RNA, and protein synthesis, and inhibition of certain enzymes. One emerging technique for the study of such mechanisms is dual polarisation interferometry. In contrast to many conventional antibiotics these peptides appear to be bactericidal instead of bacteriostatic.</p> | ||
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| + | [[File:NYMU_Group6_AMP-1.png|350px]] [[File:NYMU Group6 AMP-2.png|350px]] | ||
*See more("articles & pictures" modified from) [http://en.wikipedia.org/wiki/Antimicrobial_peptides http://en.wikipedia.org/wiki/Antimicrobial_peptides] | *See more("articles & pictures" modified from) [http://en.wikipedia.org/wiki/Antimicrobial_peptides http://en.wikipedia.org/wiki/Antimicrobial_peptides] | ||
Latest revision as of 16:23, 15 October 2018
Defensin1
Defensin is a grand group of antimicrobial peptides, having numerous kinds of similar AMPs. They are labeled by numbers, from species to species, as their identification. Different from well-studied Defensins secreted from human, our Defensin1 from honey bee has many unclear properties. Even so, its effectiveness against microbes has been proved through some stable papers.
Importantly, the sequence here is the mature peptide sequence because there are some introns which are barriers for E. coli to transcript genes in the genome DNA. That is to say, it is better to synthesize the gene through designing primers(about two sets >> four primers) as modules for real PCR. Comparatively, purifying genes & proteins from bees' genome DNA extraction is a more complicated and time-consuming method.
Basic part used in BBa_K2834005
Working Mechanism(the same as normal antimicrobial peptides)
The cytoplasmic membrane is a frequent target, but peptides may also interfere with DNA and protein synthesis, protein folding, and cell wall synthesis. The initial contact between the peptide and the target organism is electrostatic, as most bacterial surfaces are anionic, or hydrophobic. Their amino acid composition, amphipathicity, cationic charge and size allow them to attach to and insert into membrane bilayers to form pores by ‘barrel-stave’, ‘carpet’ or ‘toroidal-pore’ mechanisms. Alternately, they may penetrate into the cell to bind intracellular molecules which are crucial to cell living. Intracellular binding models includes inhibition of cell wall synthesis, alteration of the cytoplasmic membrane, activation of autolysin, inhibition of DNA, RNA, and protein synthesis, and inhibition of certain enzymes. One emerging technique for the study of such mechanisms is dual polarisation interferometry. In contrast to many conventional antibiotics these peptides appear to be bactericidal instead of bacteriostatic.
- See more("articles & pictures" modified from) [http://en.wikipedia.org/wiki/Antimicrobial_peptides http://en.wikipedia.org/wiki/Antimicrobial_peptides]
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 135
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]