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Biomimetic Material Solutions for the Stabilization of Labile Reagents

Award Information
Agency: Department of Defense
Branch: Air Force
Contract: FA8650-15-M-5005
Agency Tracking Number: F15A-T29-0221
Amount: $150,000.00
Phase: Phase I
Program: STTR
Solicitation Topic Code: AF15-AT29
Solicitation Number: 2015.1
Timeline
Solicitation Year: 2015
Award Year: 2015
Award Start Date (Proposal Award Date): 2015-06-15
Award End Date (Contract End Date): 2016-06-15
Small Business Information
401 E. State Street Suite 202B
Ithaca, NY 14850
United States
DUNS: 79535190
HUBZone Owned: Yes
Woman Owned: Yes
Socially and Economically Disadvantaged: Yes
Principal Investigator
 Jessica Felhofer
 Principal Scientist
 (607) 272-0089
 jfelhofer@carrerabio.com
Business Contact
 Patrick Govang
Title: Ms
Phone: (607) 272-0089
Email: pgovang@carrera.com
Research Institution
 Cornell University
 Gladys Chan
 
Sponsored Financial Services PO Box 22
Ithaca, NY 14851
United States

 (607) 255-8347
 Domestic Nonprofit Research Organization
Abstract

ABSTRACT: A platform (PHA-fuse) for the stabilization of diagnostic and therapeutic reagents will be established based upon the polymer, polyhydroxyalkanoate (PHA). Fusions of a target molecule to PHA synthase, the enzyme responsible for PHA synthesis, will be constructed and used to catalyze the synthesis of PHA granules. These PHA granules will help stabilize the fused target molecules and eliminate the need for cold storage. The PHA-fuse platform will be tested using a therapeutic enzyme, organophosphorus hydrolase (OPH) which is potentially valuable treatment for exposure to chemical warfare agents. In addition, an antimicrobial peptide will be tested using the PHA-fuse platform and the stability of this target along with OPH will be evaluated over time at 40oF. The PHA-fuse will be capable of stabilizing a wide array of different target molecules and will be amenable to production using a yeast host system.; BENEFIT: The PHA-fuse platform will be amenable to a wide array of target molecules through fusion to a protein that will generate a hydrophobic granule. The system will permit the stabilization and immobilization of catalysts and small molecules. The granule will be biodegradable and able to be used for diagnostic and therapeutic applications.

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

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