Difference between revisions of "Part:BBa K4248013"

 
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pET28a- T7 pro-6His -Sparamosin26-54-T7 ter
 
pET28a- T7 pro-6His -Sparamosin26-54-T7 ter
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==contribution==
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Penicillin is the first anti-infective drug used in clinical practice in the world. After years of development, more and more antibiotics have sprung up, but the problem of drug resistance caused by the large-scale and large-scale use of antibiotics has gradually become prominent. . Antibacterial peptides are considered to have broad application prospects due to their high antibacterial activity, wide antibacterial spectrum, wide variety, wide selection range, and difficulty in producing resistance mutations in target strains. The most prevalent mechanism of action of antimicrobial peptides is through their direct activity on bacterial cell membranes. Briefly, antimicrobial peptide binding leads to disruption of membrane potential, alteration of membrane permeability, and leakage of metabolites, ultimately leading to bacterial cell death. Through literature research, we found a variety of other novel antimicrobial peptides, one of which is Sparamosinsub26-54. We uploaded its DNA sequence information and basic introduction information into the registry of standard biological parts, and did the corresponding molecular construction to provide more antimicrobial peptide choices for future iGEM teams.
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[[File:T--Shanghai city-- BBa K4248013-figure1.png|500px|thumb|center| Figure 1. The map of the recombinant plasmids pET28a(+)-Sparamosin26-54 .]]
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<!-- Add more about the biology of this part here
 
<!-- Add more about the biology of this part here

Revision as of 08:19, 26 September 2022


pET28a- T7 pro-6His -Sparamosin26-54-T7 ter

pET28a- T7 pro-6His -Sparamosin26-54-T7 ter

contribution

Penicillin is the first anti-infective drug used in clinical practice in the world. After years of development, more and more antibiotics have sprung up, but the problem of drug resistance caused by the large-scale and large-scale use of antibiotics has gradually become prominent. . Antibacterial peptides are considered to have broad application prospects due to their high antibacterial activity, wide antibacterial spectrum, wide variety, wide selection range, and difficulty in producing resistance mutations in target strains. The most prevalent mechanism of action of antimicrobial peptides is through their direct activity on bacterial cell membranes. Briefly, antimicrobial peptide binding leads to disruption of membrane potential, alteration of membrane permeability, and leakage of metabolites, ultimately leading to bacterial cell death. Through literature research, we found a variety of other novel antimicrobial peptides, one of which is Sparamosinsub26-54. We uploaded its DNA sequence information and basic introduction information into the registry of standard biological parts, and did the corresponding molecular construction to provide more antimicrobial peptide choices for future iGEM teams.

Figure 1. The map of the recombinant plasmids pET28a(+)-Sparamosin26-54 .


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal NheI site found at 4598
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BglII site found at 4402
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal NgoMIV site found at 2622
    Illegal NgoMIV site found at 2782
    Illegal NgoMIV site found at 4370
  • 1000
    COMPATIBLE WITH RFC[1000]