SBIR-STTR Award

Design and Production of IgG Fc Carrier Scaffolds with Increased Payload Capacity
Award last edited on: 12/28/2023

Sponsored Program
SBIR
Awarding Agency
NSF
Total Award Amount
$1,111,368
Award Phase
2
Solicitation Topic Code
BC
Principal Investigator
David I Rabuka

Company Information

Redwood Bioscience Inc

5703 Hollis Street
Emeryville, CA 94608
   (510) 343-6031
   info@redwoodbioscience.com
   www.redwoodbioscience.com
Location: Single
Congr. District: 13
County: Alameda

Phase I

Contract Number: 1042676
Start Date: 1/1/2011    Completed: 6/30/2011
Phase I year
2010
Phase I Amount
$150,000
This Small Business Innovation Research (SBIR) Phase I project will begin to address some of the current challenges in peptide drug delivery and chemical protein conjugation. Using Redwood Bioscience's patented technology platform, a protein engineering technique, it is possible to insert a non-canonical amino acid containing a unique handle into any protein of interest. This unique handle, an "aldehyde tag", can be specifically elaborated chemically with a synthetic therapeutic peptide, for example. At Redwood Bioscience, this protein engineering technology is used to generate universal protein scaffolds, IgG Fc domains, that are easy to chemically elaborate, result in a homogenous product and can be used as long lasting protein-peptide therapies. Importantly, using this technology it is possible to elaborate the protein scaffolds with multiple tags for small molecule attachment, increasing the potential payload capacity of the carrier scaffold. The broader/commercial impact of this research is the development of best in class therapeutics with increased payload capacity and the resulting delivery of sufficiently high concentrations of a desired drug. This is a significant and substantial improvement over the current technologies available. Moreover, through expanding the chemical space of protein drugs, Redwood's technology has application in developing novel hybrid drugs with unique protein-chemical architectures, including multivalent constructs with enhanced payload capacity. The company plans to expand its pipeline of best in class therapeutic compounds, loading Fc scaffold carrier proteins with peptide or small molecule candidates, identified as potential therapeutics currently suffering from poor PK profiles

Phase II

Contract Number: 1151234
Start Date: 4/1/2012    Completed: 5/31/2016
Phase II year
2012
(last award dollars: 2014)
Phase II Amount
$961,368

This Small Business Innovation Research (SBIR) II project outlines in vivo testing of semi-synthetic therapeutic protein conjugates. Low molecular weight peptide drugs have had limited therapeutic utility due to rapid clearance and, consequently must be injected very frequently. These drugs could be conjugated to a carrier protein. Attachment to large biomolecules, such as carrier proteins, improves the half-life profile of these peptides. Historically, many of these carrier proteins are recombinant genetic fusions with the peptide of interest. With fusion, the carrier?s attachment to the peptide is limited to one site, the end terminus, and that limited placement can impact drug function and thus potency. As an alternative, chemical modification to carrier proteins with small molecule drugs can also render the drug more potent and longer lasting. The scientists at Redwood Bioscience have developed a technology platform that can universally modify proteins in a controlled, site-specific manner. They have generated carrier protein scaffolds, modified recombinant Fc domains that are homogeneous and easy to chemically elaborate with therapeutic peptides. Furthermore, optimized peptide conjugation to the Fc proteins improves conjugate activity in vitro. This technology is to be further validated through an initial in vivo analysis. The broader impacts of this research are the development of best in class therapeutics and the generation of a robust protein modification platform. This work will change the utility of protein therapeutics by enabling optimization of therapeutic peptides that otherwise would not be useful as treatment for disease