Difference between revisions of "Part:BBa K5101000"

 
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<partinfo>BBa_K5101000 short</partinfo>
 
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Antimicrobial peptides (AMP) are a large class of active oligopeptides with antimicrobial properties against harmful life forms (or pathogens) such as bacteria, fungi, parasites and viruses. In addition to their antimicrobial ability, some of these peptides can directly or indirectly participate in the immunomodulation of the host and protect the host from infection. Because they generally have a sufficient amount of positive charge and are often accompanied by hydrophobicity, they can bind to negatively charged biological membranes under electrostatic force, penetrate and destroy the membrane structure to cause cell death. Different from the traditional antibiotic single-target sterilization principle, antimicrobial peptide can carry out multi-target destruction in pathogens, which can greatly reduce the production of drug-resistant bacteria, and has a broad-spectrum antimicrobial properties, which is one of the best choices for replacing antibiotics in the future. In the current global situation, antimicrobial peptides have been used in many clinical treatment cases in bacterial infection, wound healing and cancer treatment. With the development of synthetic biology and biomedical engineering and other interdisciplinary disciplines, the molecular design and biosynthesis of antimicrobial peptides will have more ideas and technical support. Imbalance of intestinal flora and loss of tolerance to local microbiota are possible causes of inducing chronic enteritis. Therefore, regulating the balance of intestinal flora can help alleviate intestinal inflammation and improve the therapeutic effect of chronic enteritis.
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Antimicrobial peptide ORF
We constructed suitable engineered bacterial strains to characterize a novel antimicrobial peptide newly isolated from Lactobacillus from the human vaginal flora in our Host lab (unpublished data). The antimicrobial peptide has been shown to have some bacteriostatic properties after validation with our constructed engineered bacteria. It has a wide range of bacteriostatic activity against Gram-positive and Gram-negative bacteria.
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===Usage and Biology===
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<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>
 
<partinfo>BBa_K5101000 SequenceAndFeatures</partinfo>
 
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<partinfo>BBa_K5101000 parameters</partinfo>
 
<partinfo>BBa_K5101000 parameters</partinfo>
 
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===Profile===
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<br>Base Pairs: 228 bp
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<br>Origin: Lactobacilli in the human vaginal flora
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<br>Properties: Antimicrobial peptide that has an antibacterial effect
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===Usage and Biology===
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Antimicrobial peptides (AMP) are a large class of active oligopeptides with antimicrobial properties against harmful life forms (or pathogens) such as bacteria, fungi, parasites and viruses. In addition to their antimicrobial ability, some of these peptides can directly or indirectly participate in the immunomodulation of the host and protect the host from infection. Because they generally have a sufficient amount of positive charge and are often accompanied by hydrophobicity, they can bind to negatively charged biological membranes under electrostatic force, penetrate and destroy the membrane structure to cause cell death. Different from the traditional antibiotic single-target sterilization principle, antimicrobial peptide can carry out multi-target destruction in pathogens, which can greatly reduce the production of drug-resistant bacteria, and has a broad-spectrum antimicrobial properties, which is one of the best choices for replacing antibiotics in the future. In the current global situation, antimicrobial peptides have been used in many clinical treatment cases in bacterial infection, wound healing and cancer treatment. With the development of synthetic biology and biomedical engineering and other interdisciplinary disciplines, the molecular design and biosynthesis of antimicrobial peptides will have more ideas and technical support. Imbalance of intestinal flora and loss of tolerance to local microbiota are possible causes of inducing chronic enteritis. Therefore, regulating the balance of intestinal flora can help alleviate intestinal inflammation and improve the therapeutic effect of chronic enteritis.
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We constructed suitable engineered bacterial strains to characterize a novel antimicrobial peptide newly isolated from Lactobacillus from the human vaginal flora in our Host lab (unpublished data). The antimicrobial peptide has been shown to have some bacteriostatic properties after validation with our constructed engineered bacteria. It has a wide range of bacteriostatic activity against Gram-positive and Gram-negative bacteria.

Revision as of 04:39, 3 August 2024


Antimicrobial peptide discoverd from the Lactobacilli in the human vaginal flora

Antimicrobial peptide ORF

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
    INCOMPATIBLE WITH RFC[25]
    Illegal AgeI site found at 199
  • 1000
    COMPATIBLE WITH RFC[1000]