Difference between revisions of "Part:BBa K3096016"
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TAT-LK15 is a short fusion peptide of the cell-penetrating peptide (CPP) Tat and the synthetic LK15 peptide. Adding LK15 to Tat results in improved transport efficiency across the cell membrane. The part has been reported to be able to transport nucleic acids through membranes, which allows for novel transfection protocols. LK15 consists of 15 amino acids, which are all either leucine (L) or lysine (K) residue, resulting in an amphipathic protein. | TAT-LK15 is a short fusion peptide of the cell-penetrating peptide (CPP) Tat and the synthetic LK15 peptide. Adding LK15 to Tat results in improved transport efficiency across the cell membrane. The part has been reported to be able to transport nucleic acids through membranes, which allows for novel transfection protocols. LK15 consists of 15 amino acids, which are all either leucine (L) or lysine (K) residue, resulting in an amphipathic protein. | ||
− | The improved activity of TAT-LK15 over the Tat was also confirmed by our CPP transport activity prediction tool C3Pred. TAT-LK15 scored significantly | + | The improved activity of TAT-LK15 over the Tat was also confirmed by our CPP transport activity prediction tool C3Pred. TAT-LK15 scored significantly than the wildtype Tat. This can partly be explained by the presence of multiple positively charged residues in the LK15 peptide, which have been shown to associated with high transport efficiency by our software tool. |
===Sequence and Features=== | ===Sequence and Features=== |
Revision as of 09:31, 16 October 2019
Tat-LK15 - improved Cell penetrating peptide
TAT-LK15 is a short fusion peptide of the cell-penetrating peptide (CPP) Tat and the synthetic LK15 peptide. Adding LK15 to Tat results in improved transport efficiency across the cell membrane. The part has been reported to be able to transport nucleic acids through membranes, which allows for novel transfection protocols. LK15 consists of 15 amino acids, which are all either leucine (L) or lysine (K) residue, resulting in an amphipathic protein.
The improved activity of TAT-LK15 over the Tat was also confirmed by our CPP transport activity prediction tool C3Pred. TAT-LK15 scored significantly than the wildtype Tat. This can partly be explained by the presence of multiple positively charged residues in the LK15 peptide, which have been shown to associated with high transport efficiency by our software tool.
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]
References
- Saleh, Amer F., et al. "Improved Tat-mediated plasmid DNA transfer by fusion to LK15 peptide." Journal of Controlled Release 143.2 (2010): 233-242.