Open AccessThis article is
- freely available
Targeted Secretion Inhibitors—Innovative Protein Therapeutics
Syntaxin Ltd, Units 4-10 The Quadrant, Barton Lane, Abingdon, OXON, OX14 3YS, UK
* Author to whom correspondence should be addressed.
Received: 15 October 2010; in revised form: 16 November 2010 / Accepted: 2 December 2010 / Published: 3 December 2010
Abstract: Botulinum neurotoxins are highly effective therapeutic products. Their therapeutic success results from highly specific and potent inhibition of neurotransmitter release with a duration of action measured in months. These same properties, however, make the botulinum neurotoxins the most potent acute lethal toxins known. Their toxicity and restricted target cell activity severely limits their clinical utility. Understanding the structure-function relationship of the neurotoxins has enabled the development of recombinant proteins selectively incorporating specific aspects of their pharmacology. The resulting proteins are not neurotoxins, but a new class of biopharmaceuticals, Targeted Secretion Inhibitors (TSI), suitable for the treatment of a wide range of diseases where secretion plays a major role. TSI proteins inhibit secretion for a prolonged period following a single application, making them particularly suited to the treatment of chronic diseases. A TSI for the treatment of chronic pain is in clinical development.
Keywords: botulinum neurotoxins; biologics; protein therapeutics; recombinant proteins; genetic engineering; SNARE proteins
Article StatisticsClick here to load and display the download statistics.
Notes: Multiple requests from the same IP address are counted as one view.
Cite This Article
MDPI and ACS Style
Keith, F.; John, C. Targeted Secretion Inhibitors—Innovative Protein Therapeutics. Toxins 2010, 2, 2795-2815.
Keith F, John C. Targeted Secretion Inhibitors—Innovative Protein Therapeutics. Toxins. 2010; 2(12):2795-2815.
Keith, Foster; John, Chaddock. 2010. "Targeted Secretion Inhibitors—Innovative Protein Therapeutics." Toxins 2, no. 12: 2795-2815.