Difference between revisions of "Part:BBa K4221006"
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===Biology=== | ===Biology=== | ||
LL-37 is a C-terminal cleavage product of Cathelicidin peptide HCAP-18, which can directly kill bacteria, fungi and viruses. | LL-37 is a C-terminal cleavage product of Cathelicidin peptide HCAP-18, which can directly kill bacteria, fungi and viruses. | ||
| − | Design Consideration | + | |
| + | ===Design Consideration=== | ||
The construction includes: | The construction includes: | ||
| − | LL37 is fused with BslA with a GS | + | |
| + | LL37 is fused with BslA with a GS linker（GGTGGTGGCGGCAGCGGCGGAGGCGGTAGT） | ||
===Reference=== | ===Reference=== | ||
Latest revision as of 15:53, 10 October 2022
LL37
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE 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（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)