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Patent
Synaptic Research, Llc and Johns Hopkins University | Date: 2011-08-16

The present invention provides methods for the isolation of oils from intact or lysed microorganisms in aqueous media with pressurized carbon dioxide as a solute. Such oils may be used for the production of biofuels. Also provided for are methods for harvesting and rupturing whole cell microorganisms in aqueous media with pressurized carbon dioxide as a solute


Patent
Synaptic Research, Llc | Date: 2013-06-25

The invention provides eukaryotic unicellular algae engineered to express a nucleosome alteration protein fused to a protein with affinity to the DNA binding site acting in coordination. An example is a LexA-p300 fusion protein, where the p300 is derived from Chlamydomonas. The LexA binding domain guides the p300 to the binding site and the p300 loosens the nucleosome structure by acetylating histones within proximity of the transgene, thus remodeling the local chromatin structure to allow for high-level expression.


A novel protein delivery system to generate induced pluripotent stem (iPS) cells is described. The delivery system comprises a construct with a receptor binding domain that recognizes a receptor in a somatic cell, a translocation domain that allows the transfer of an inducer into the cytosolic space, and a cargo bearing domain to which the inducer is attached and facilitates transfer of the inducer into the cell.


Grant
Agency: Department of Energy | Branch: | Program: SBIR | Phase: Phase II | Award Amount: 998.54K | Year: 2011

One of the principal technical and cost barriers to successful commercialization of algal biofuels as an alternative energy source is the inability to extract the useful oil components from the algae in an economical and environmentally sound fashion. Indeed, the DOE announcement for this proposal specifically notes topic areas (5d) regarding methods for extracting oils from microalgae as goal of research and development. The announcement further recognizes the critical barriers that impact cost and performance: oil extraction systems for wet algal biomass and further purification of neutral lipids. Current processing methods for algal oil require large investments in costly and energy intensive centrifuges and distillation equipment using environmentally unfriendly solvents such as hexane due to the difficulty in isolating oil components from residual biomass and water. Alternative strategies are urgently needed to purify the valuable oil components from algae that can be subsequently processed into useful biodiesel. The objective of this Phase I/Phase II project is to implement a novel chemical processing strategy that applies carbon dioxide as a solute to alter the physical properties of lipids including density, viscosity, and solubility such that algal oil is more readily separated from the remaining biomass and water. Our CO2 solute enhanced lipid isolation is fundamentally different from supercritical extraction, which uses CO2 as a solvent and requires much greater volumes of CO2 and high capital costs. During Phase I, we measured the effects of CO2 on the physical properties of oil, water, and algal biomass in a series of laboratory experiments. Significant CO2 solute dissolves primarily in oil as a single phase at elevated pressures to alter the density and viscosity of oil and facilitates the separation of oil from separate phases of algal biomass and water. Therefore, the aim of the proposed Phase II project is to translate this knowledge of physical properties of CO2 solute in oil into a complete chemical process for purifying oil from biomass and water at laboratory scale. During year 1, optimal process operating parameters will be specified for the specific unit operations in order to reduce the water content following algal growth, solubilize CO2 solute in oil, purify oil from biomass and water, then recycle the CO2 and water. The second year of the Phase II project will integrate these individual unit operations into a continuous process and to design an economical process for scale up in Phase III. The Phase III project, if approved, will implement a pilot project at 200-to 2,000-fold higher scales that demonstrates the commercial feasibility of CO2 solute based processing for oil purification from algal biomass and water. Commercial Applications & amp; Other Benefits: The commercial benefits will be a substantial reduction in processing costs for purifying oil from algal biomass. As processing the algal species represents the single highest capital cost component of algal biofuels, methodologies that reduce these costs will have a significant impact towards making algal biofuels including biodiesel and other products economically viable. Given the expanding number of algal growth companies in the US, the implementation of complementary technologies to process the algae to oil and residual biomass represents an equally important goal towards the development of a commercially viable renewal algal biofuels source to replace current fossil fuels.


Patent
Synaptic Research, Llc and The Regents Of The University Of California | Date: 2012-10-26

This invention provides diatom-based vaccines.


Grant
Agency: Department of Health and Human Services | Branch: | Program: SBIR | Phase: Phase I | Award Amount: 324.52K | Year: 2011

DESCRIPTION (provided by applicant): Induced pluripotent stem cells (iPSC) have tremendous potential for regenerative medicine in future. However, there are obstacles to overcome before the iPSC can be used therapeutically. One major hurdle is the tool used to generate iPSC from adult somatic cells. We believe that the delivery of reprogramming proteins directly rather than the genes that encode these proteins is the safest means for generating iPSC. We propose to engineer Clostridium difficile toxin TcdB as a cytosolic delivery vehicle for embryonic transactivators that can reprogram adult somatic cells to induced pluripotent stem cells (iPSC) and/or tissue specific cells. C. difficile toxin TcdB, exhibits multiple modular domains that provide all the mechanisms that allow the toxin efficiently deliver its N-terminal enzymatic domain (GT domain) to cytosol. We will engineer TcdB as a universal protein delivery vehicle by replaceing the enzymatic domain with a protein cargo to provide therapeutic benefits.We will initially append a chimeric transacivator to the N-terminus of the toxin or replace the GT domain with the chimeric transactivator. Using a high-throughput reporter cell line system, we will first examine how effectively the engineered recombinantprotein can deliver a biologically active cargo. We will then test if the engineered TcdB can deliver biologically active reprogramming factors (Oct4 and Sox2) to another reporter cell line and assess their ability to differentiate mouse embryonic stem cells with the help of our collaborators. Finally, we will use the TcdB delivery vehicle to generate of iPSC from mouse embryonic fibroblasts after we demonstrate that we can deliver those reprogramming factors efficiently to the well-characterized reportercells. Other methods of delivering proteins, such as the TAT protein transduction domain, will be tested in parallel to compare the efficiency of our novel system to established techniques. We believe this TcdB-based protein delivery vehicle will be a valuable tool for generating iPSC for research purposes, drug development, and toxicology studies. We also anticipate the development of TcdB-based biologics for regenerative medicine. PUBLIC HEALTH RELEVANCE: This project will investigate the use of anew protein delivery vehicle to introduce reprogramming factors to adult skin cells in order to convert them to induced pluripotent stem cells (iPSC). This approach relies on proteins rather than genes to create iPSC, which avoids the potential dangers ofgenetic modification. These iPSC have enormous potential to replace embryonic stem cells for regenerative medicine.


Patent
Synaptic Research, Llc | Date: 2015-01-27

A cell based assay for detection for protease activity is disclosed. In the assay a cell is engineered to express a protease substrate with at least one label, preferably on its C-terminus. Cleavage of the substrate by the protease that recognizes it results in a C-terminal fragment and a N-terminal fragment, where the fragment having the label is subject to ubiquitin proteasome degradation. The assay measures the disappearance of the label due to degradation of the fragment to which it is attached. A cell free assay is also described for detection of protease activity. In the cell free assay, the protease substrate is expressed in a solution that includes the elements of the ubiquitin proteasome pathway for degradation of the fragment. The assay measures the disappearance of the label attached to the fragment that results from cleavage by the protease.


The present invention relates to a designer or recombinant ubiquitin ligase molecule that includes a toxin binding domain that is specific for a toxin active fragment, wherein the toxin active fragment is an enzymatically active fragment of one or more toxins or toxin serotypes; and an E3-ligase domain that comprises an E3-ligase or polypeptide that facilitates E2-mediated ubiquitination of the toxin active fragment. In an embodiment, the composition further includes a delivery system that allow the designer ubiquitin ligase to enter the cell. The present invention further includes methods for treating an individual intoxicated with a toxin by administering the designer ubiquitin ligase of the present invention.


Patent
Synaptic Research, Llc | Date: 2011-06-13

A cell based assay for detection for protease activity is disclosed. In the assay a cell is engineered to express a protease substrate with at least one label, preferably on its C-terminus. Cleavage of the substrate by the protease that recognizes it results in a C-terminal fragment and a N-terminal fragment, where the fragment having the label is subject to ubiquitin proteasome degradation. The assay measures the disappearance of the label due to degradation of the fragment to which it is attached. A cell free assay is also described for detection of protease activity. In the cell free assay, the protease substrate is expressed in a solution that includes the elements of the ubiquitin proteasome pathway for degradation of the fragment. The assay measures the disappearance of the label attached to the fragment that results from cleavage by the protease.


A system for the identification of proteases and protease inhibitors is provided. The system has at least two components. The first component is a reporter construct with at least one binding site, a transcriptional promoter, an inducible promoter region, and at least one reporter gene, all functionally connected for expression of the reporter gene(s) in functional coordination with a transcriptional activation agent. The second component is a transcriptional activation agent comprising a nucleic acid binding domain, at least one protease substrate domain, and at least one transcriptional activation domain for an inducible promoter. The system allows detection and evaluation of agents affecting protease activity directed to the protease substrate domain. The system also allows for the detection of the presence of proteases in environmental samples.

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