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STTR Phase I: Novel Production Platform for Synthesis of Toxic Enzymes

Award Information
Agency: National Science Foundation
Branch: N/A
Contract: 0740643
Agency Tracking Number: 0740643
Amount: $150,000.00
Phase: Phase I
Program: STTR
Solicitation Topic Code: BT
Solicitation Number: NSF 07-551
Timeline
Solicitation Year: N/A
Award Year: 2008
Award Start Date (Proposal Award Date): N/A
Award End Date (Contract End Date): N/A
Small Business Information
13328 Manor Stone Drive
Germantown, MD 20874
United States
DUNS: 608276296
HUBZone Owned: No
Woman Owned: Yes
Socially and Economically Disadvantaged: No
Principal Investigator
 Aprile Pilon
 DPhil
 (301) 452-2899
 apilon@apcbio.com
Business Contact
 Aprile Pilon
Title: DPhil
Phone: (301) 452-2899
Email: apilon@apcbio.com
Research Institution
 Princeton University
 David Wood
 
E-Quad
Princeton, NJ 8544
United States

 (301) 452-2899
 Nonprofit College or University
Abstract

This Small Business Technology Transfer Phase I research develops a novel bioprocess platform for the synthesis of toxic enzymes as inactive pro-enzymes in bacteria that can subsequently be activated via simple pH and/or temperature shifts. Recombinant enzymes for industrial synthetic applications or pharmacologic replacement therapies can be very difficult and expensive to produce in large quantities in an active form because they are toxic to the host, self-inactivate, or both. Numerous proteases, digestive enzymes, and cross-linking enzymes that break down or build up macromolecular complexes with high commercial potential are all but impossible to isolate in active form. The company proposes to use the catalytic core of the human transglutaminase 1 enzyme (TG1) to prove the concept. This research could have a direct impact on patients suffering from a severe form of ?scaly skin? disease, known as lamellar icthyosis, who have a defect in their TG1 gene. The broader impacts of this research are development of novel biomaterials and/or processes for several industries, including biotechnology, food processing, cosmetics and skin care (non-pharmacologic), detergents, and possibly waste remediation. Recombinant transglutaminases will specifically enable the development of novel types of biopolymers and materials. The research with TG1 could have a broader impact in the biomedical industry because it may lead to the development of a TG1-based ?liquid bandage? product for use in treatment of wounds, burns and cosmetic/reconstructive surgeries.

* Information listed above is at the time of submission. *

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