Difference between revisions of "Part:BBa K4221017"

(Design Consideration)
 
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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  
 
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  
  
Our team used the amphiphilicity of BslA to enhance the antibacterial/targeting effect of LL37 antimicrobial peptide and RGD-targeted peptide
+
Our team used the amphiphilicity of BslA to enhance the antibacterial/targeting effect of LL37 antimicrobial peptide
  
 
===Biology===
 
===Biology===

Latest revision as of 06:44, 11 October 2022


LL37-GSlinker-BslA(42-181aa)

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

Our team used the amphiphilicity of BslA to enhance the antibacterial/targeting effect of LL37 antimicrobial peptide

Biology

LL-37 is a C-terminal cleavage product of Cathelicidin peptide HCAP-18, which can directly kill bacteria, fungi and viruses.

BslA is a structurally defined bacterial hydrophobin that was found in the biofilm of Bacillus subtilis. It helps the assembling of TasA (an exopolysaccharide and an amyloid fiber-forming protein), the component of the biofilm matrix. BslA is composed of an Ig-type fold with the addition of an unusual, extremely hydrophobic “cap” region. The central hydrophobic residues of the cap are essential to allow a hydrophobic, nonwetting biofilm to form as they control the surface activity of the BslA protein.[2]

Design Consideration

The construction includes:

LL37 is fused with BslA with a GS linker(GGTGGTGGCGGCAGCGGCGGAGGCGGTAGT)

Reference

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

[2]: “BslA is a self-assembling bacterial hydrophobin that coats the Bacillus subtilis biofilm.” Proceedings of the National Academy of Sciences of the United States of America vol. 110,33 (2013): 13600-5. doi:10.1073/pnas.1306390110