Overview
Syntaxin has developed a proprietary technology to create novel recombinant proteins termed Targeted Secretion Inhibitors (TSI).
These engineered molecules are selectively able to deliver an endopeptidase into defined target cells and specifically cleave SNARE proteins driving secretion from that cell. This technology is based upon the endopeptidase activity found within clostridial neurotoxins, which cleaves SNARE proteins and inhibits vesicular cell secretion.
TSI are potent and have the potential to be administered both locally and systemically with duration of action from weeks to months from a single dose. They have potential in the treatment of a wide range of diseases involving cell secretion.
By specifically inhibiting inappropriate or aberrant secretion from target cells, Syntaxin’s TSI represent a major new class of protein biotherapeutic.
Inhibition of Cell Secretion
Clostridial neurotoxins, including the botulinum neurotoxin (BoNTs), are proteases that selectively cut one of the soluble N-ethylmaleimidesensitive factor attachment protein receptor (SNARE) proteins involved in regulated secretion.
Creating Novel Proteins
The clostridial neurotoxins all consist of two peptide chains covalently linked by a disulphide bridge with a highly conserved domain structure related to function.
Therapeutic Potential
The ability to develop novel recombinant proteins able to deliver a clostridial or tetanus neurotoxin protease into a cell of choice and thereby inhibit vesicle fusion and secretion from the selected target cell with prolonged duraction of action.