Provided herein are modified caspase-9 polypeptides, and chimeric caspase-9 proteins containing the modified caspase-9 polypeptides. The disclosure further provides polynucleotides encoding these proteins, engineered host cells containing these polynucleotides and proteins, including host cells that co-express a chimeric antigen receptor, and methods of making and using the same.

A method of forming a stable protein complex comprising: providing aqueous protein complexes, wherein the protein complexes are one or more of photosystem I complex from spinach, photosystem II complex from spinach, chlorophyll antennae, thylakoids, bacteriochlorophylls, chlorosomes, and photosystems from green algae, cyanobacteria, and plants; cationizing the aqueous protein complexes by the addition of stoichiometric amounts of a crosslinker in the presence of a coupling reagent; titrating the cationized protein complexes with a counter anionic polymer until the protein cation/anion pair solution becomes negative by zeta potential measurement, to create at least one antibody cation/anion pair in aqueous solution. The protein complexes cation/anion pair solution may be lyophilized to remove all of the water, forming a lyophilized solid. The lyophilized solid may be heated until a protein complex ionic liquid is generated. The cationized protein complexes may be purified from excess coupling reagents by dialysis in water.

A method of forming a stable protein complex comprising: providing aqueous protein complexes, wherein the protein complexes are one or more of photosystem I complex from spinach, photosystem II complex from spinach, chlorophyll antennae, thylakoids, bacteriochlorophylls, chlorosomes, and photosystems from green algae, cyanobacteria, and plants; cationizing the aqueous protein complexes by the addition of stoichiometric amounts of a crosslinker in the presence of a coupling reagent; titrating the cationized protein complexes with a counter anionic polymer until the protein cation/anion pair solution becomes negative by zeta potential measurement, to create at least one antibody cation/anion pair in aqueous solution. The protein complexes cation/anion pair solution may be lyophilized to remove all of the water, forming a lyophilized solid. The lyophilized solid may be heated until a protein complex ionic liquid is generated. The cationized protein complexes may be purified from excess coupling reagents by dialysis in water.

A detoxification method includes the steps of inducing flow of patient blood through an extracorporeal device inlet and outlet in fluid connection to the circulatory system of a patient. Biological agents including lipopolysaccharide (LPS) contained within patient blood can be detoxified by passing patient blood over a biochemical reactor surface having attached or immobilized Saccharomyces boulardii alkaline phosphatase enzyme, with the biochemical reactor being contained within the extracorporeal device. An acyloxyacyl hydrolase enzyme may also be used on the biochemical reactor surface.

A detoxification method includes the steps of inducing flow of patient blood through an extracorporeal device inlet and outlet in fluid connection to the circulatory system of a patient. Biological agents including lipopolysaccharide (LPS) contained within patient blood can be detoxified by passing patient blood over a biochemical reactor surface having attached or immobilized Saccharomyces boulardii alkaline phosphatase enzyme, with the biochemical reactor being contained within the extracorporeal device. An acyloxyacyl hydrolase enzyme may also be used on the biochemical reactor surface.

A nanostructure is provided having a protein shell comprising one or more proteins, at least one nucleic acid scaffold with a plurality of nucleic acid recognition sequences configured to bind to a plurality of enzymes and a plurality of nucleic acid spacers between the plurality of nucleic acid recognition sequences, a linkage between the at least one nucleic acid scaffold and the protein shell, and the plurality of enzymes that are at least partially complementary to the at least one nucleic acid scaffold, each enzyme comprising a nucleic acid binding domain configured to bind the enzyme and the at least one nucleic acid scaffold with some degree of molecular complementarity.

The present invention provides devices and methods for producing metabolites used to measure the toxicity of chemical compounds. They incorporate enzymatic microsomes and magnetic nanoparticles that magnetically entrap enzymes. These enzyme systems catalyze chemicals to yield measurable metabolic products. The microsomes and the magnetic nanoparticles containing enzymes are associated with macroporous scaffolds and non-reactive components that facilitate the enzyme reactions.

The present invention provides devices and methods for producing metabolites used to measure the toxicity of chemical compounds. They incorporate enzymatic microsomes and magnetic nanoparticles that magnetically entrap enzymes. These enzyme systems catalyze chemicals to yield measurable metabolic products. The microsomes and the magnetic nanoparticles containing enzymes are associated with macroporous scaffolds and non-reactive components that facilitate the enzyme reactions.

A detoxification method includes the steps of inducing flow of patient blood through an extracorporeal device inlet and outlet in fluid connection to the circulatory system of a patient. Biological agents including lipopolysaccharide (LPS) contained within patient blood can be detoxified by passing patient blood over a biochemical reactor surface having attached or immobilized Saccharomyces boulardii alkaline phosphatase enzyme, with the biochemical reactor being contained within the extracorporeal device.

A detoxification method includes the steps of inducing flow of patient blood through an extracorporeal device inlet and outlet in fluid connection to the circulatory system of a patient. Biological agents including lipopolysaccharide (LPS) contained within patient blood can be detoxified by passing patient blood over a biochemical reactor surface having attached or immobilized Saccharomyces boulardii alkaline phosphatase enzyme, with the biochemical reactor being contained within the extracorporeal device.