Difference between revisions of "Part:BBa K4221006"

 
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<partinfo>BBa_K4221006 short</partinfo>
 
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===Usage and Biology===
 
  
 
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<partinfo>BBa_K4221006 parameters</partinfo>
 
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===Usage===
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The search for new approaches for developing antimicrobial surfaces is a challenge of great urgency to prevent and control microbial growth on surfaces. 
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Our team design of a new, simple and general tool for creating antimicrobial surfaces, based on use a hydrophobin protein BslA to replaced the hydrophobin Vmh2 from Pleurotusostreatus to the human antimicrobial peptide
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===Biology===
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LL-37 is a C-terminal cleavage product of Cathelicidin peptide HCAP-18, which can directly kill bacteria, fungi and viruses.
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Design Consideration:
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The construction includes:
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LL37 is fused with BslA with a GS linker
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===Reference===
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[1]I. Sorrentino, M. Gargano, A. Ricciardelli, et al., Developmentof anti-bacterial surfaces using a hydrophobin chimeric protein, International Journal ofBiological Macromolecules (2018)
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===Usage and Biology===

Revision as of 14:39, 8 October 2022


LL37

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]


Usage

The search for new approaches for developing antimicrobial surfaces is a challenge of great urgency to prevent and control microbial growth on surfaces. Our team design of a new, simple and general tool for creating antimicrobial surfaces, based on use a hydrophobin protein BslA to replaced the hydrophobin Vmh2 from Pleurotusostreatus to the human antimicrobial peptide

Biology

LL-37 is a C-terminal cleavage product of Cathelicidin peptide HCAP-18, which can directly kill bacteria, fungi and viruses. Design Consideration: The construction includes: LL37 is fused with BslA with a GS linker

Reference

[1]I. Sorrentino, M. Gargano, A. Ricciardelli, et al., Developmentof anti-bacterial surfaces using a hydrophobin chimeric protein, International Journal ofBiological Macromolecules (2018)