Part:BBa_K3712002
Optimized BLP-7
USAGE AND BIOLOGY
Although, BLP-7 has a huge power against bacteria, its antibacterial and anti-inflammatory effects are still able to be further improved. Theoretically, increasing the net positive charge and hydrophobicity of antimicrobial peptides can improve its antibacterial ability. In this project, we carried out amino acid mutation of wild-type BLP-7 through modeling design, replaced specific amino acids to improve its hydrophobicity, so that antimicrobial peptides could better bind to bacterial cell membranes and improve its drilling ability. In this way, we expect to obtain a more stable mutant BLP-7 with better antibacterial and anti-inflammatory effects.
RESULTS
Although the modeling team has given a good verification that 27 ELP has the temperature control effect we expect, in the future we will verify the temperature control aggregation ability of 54 ELP through experiments to further support the ELP aggregation temperature of the modeling group. The applicability of the control aggregation model. Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Illegal PstI site found at 26
- 12INCOMPATIBLE WITH RFC[12]Illegal PstI site found at 26
- 21COMPATIBLE WITH RFC[21]
- 23INCOMPATIBLE WITH RFC[23]Illegal PstI site found at 26
- 25INCOMPATIBLE WITH RFC[25]Illegal PstI site found at 26
- 1000COMPATIBLE WITH RFC[1000]
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