Part:BBa_K4990009
Bacteria-Targeting Peptide
TO KNOW ABOUT IT!
In the wake of advancements in molecular biology, numerous proteins and peptides with active functions have been discovered or invented for pharmaceutical applications. Recombinant technology, characterized by its high expression levels and ease of operation, has been extensively applied in biomedicine and related fields. To obtain multi-target, multifunctional active proteins, it is requisite to link and fuse two or more proteins with known functions. This method of obtaining bifunctional or multifunctional fusion proteins has become one of the new approaches for developing new drugs and researching bioproducts, especially widely used in the preparation of bispecific single-chain variable fragments (scFv) or antibody-drug conjugates[1-5].
Fusion proteins are principally composed of two parts: the functional protein and the linker peptide. The functional protein is the original protein intended for fusion, typically with known structure and function, posing no issues in selection. However, due to the significance of the linker peptide in the overall structure of the fusion protein, its selection and design require thoughtful research to ensure the overall activity of the fusion protein remains unchanged[2]. Consequently, research on linker peptides has gradually come into focus.
Usage in short
You can use it to target and kill Fn.
What is it
This is the structure of (Bacteria-Targeting Peptide)BTP, which is consited of B-domain, Linker A, FK-13.
B-domain targets the pilus of Fn, Linker A is a rigid and cleavage linker, FK-13 has antimicrobial activity.
Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Illegal PstI site found at 31
- 12INCOMPATIBLE WITH RFC[12]Illegal PstI site found at 31
- 21COMPATIBLE WITH RFC[21]
- 23INCOMPATIBLE WITH RFC[23]Illegal PstI site found at 31
- 25INCOMPATIBLE WITH RFC[25]Illegal PstI site found at 31
- 1000COMPATIBLE WITH RFC[1000]
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