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Provides easily accessible and relatively abundant sources of human β- or γ-actin.  Background:
Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells. In vertebrates, three main groups of actin isoforms (alpha, beta and gamma) have been identified. Alpha actins are found in muscle tissues. Beta and gamma actins coexist in most cell types as components of the cytoskeleton and as mediators of internal cell motility. Biochemical studies of human actin and its binding partners rely heavily on abundant and easily purified α-actin from skeletal muscle. Therefore, muscle actin has been used to evaluate and determine the activities of most actin regulatory proteins. In addition, there is underlying concern these proteins perform differently with actin present in non-muscle cells.Technology Overview:  
This technology provides easily accessible and relatively abundant sources of human β- or γ-actin (in other words, cytoplasmic actins). The technology consists of Saccharomyces cerevisiae strains that express β- and γ- actins as their sole source of actin. Both β- or γ-actin purified in this system polymerize and interact with various binding partners, including profilin, cofilin, mDia1 (formin), fascin, and thymosin-β4 (Tβ4). Notably, Tβ4 binds to β- or γ-actin with higher affinity than to muscle α-actin, emphasizing the value of testing actin ligands with specific actin isoforms. These reagents will make specific isoforms of actin more accessible for future studies of actin regulation. https://suny.technologypublisher.com/files/sites/adobestock_588658728.jpegAdvantages:  
•    High yield.
•    No special growth requirements.
•    Requires only conventional purification reagents and protocols.
•    No additional post-purification processing.
•    No concern over removal of contaminating “host” actin. Applications:  
The primary application for this technology is to evaluate and determine the activities of actin regulatory proteins.  Intellectual Property Summary:
U.S. Provisional Patent Application No. 63/399,088 filed 8/18/22Stage of Development:
TRL 3 - Experimental proof of concept Licensing Status:
This technology is available for licensing Licensing Potential:
This technology would be of interest to anyone involved in biochemical studies of human actin and its binding partners, including:
•    Pharmaceutical companies.
•    Medical research laboratories.
•    Universities and other educational facilities.

 

A nanoparticle-based method for enhanced delivery of protein/peptide therapeutics.  Background:
Biologics, for example protein and peptide-based therapeutics, have poor in vitro shelf stability and in vivo enzymatic stability, which lead to short blood circulating time and contribute to immunogenicity. In addition, biologics are impermeable to biological barriers with poor bioavailability and cell uptake. Encapsulation of active protein inside a nanoparticle can increase stability and improve efficacy for better disease treatment in patients. Unfortunately, therapies of this type are limited by the lack of efficient carriers that improve in vivo stability, reduce immunogenicity, and can deliver the therapeutic into intracellular space while maintaining bioactivity. The goal is to create small nanoparticles (10 to 30 nm) with high protein loading ability and cell-penetration properties. However, it remains technically challenging to create particles of this size while maintaining protein loading capacity.Technology Overview:  
This technology is a novel method for protein drug delivery. The technology consists of functional segregated telodendrimers that can have two or three functional segments. The telodendrimers consist of a linear polyethylene glycol and a dendritic polylysine/polyarginine with flexible linker-conjugated hydrophobic natural compounds. These telodendrimers can associate with the protein surface for effective protein coating and encapsulation into neutral and stable sub-30 nm nanoparticles with high amounts of proteins (30 to 200% of the telodendrimer by weight). This is capable of intracellular protein delivery. The favorable physical properties and biocompatibility of the telodendrimer nanoparticles make them highly suitable as nanocarriers for protein-based therapies, such as antibodies and insulin for cancer and diabetes treatments.  https://suny.technologypublisher.com/files/sites/adobestock_465444146.jpegAdvantages:  
•    In situ protein loading.
•    No organic solvent and adjuvant free.
•    High loading capabilities.
•    Enhanced bioavailability with reduced cytotoxicity.
•    Size, capacity, and cell penetration can be adjusted.
•    Improved in vivo stability.
•    Better control over protein release.
•    Well-defined chemical structure. 
•    Improved passive tumor targeting.
 Applications:  
The primary application for this technology is protein/peptide encapsulation and delivery.  Intellectual Property Summary:
Granted Patents: US10,947,350, EP3347053Stage of Development:
TRL 3 - Experimental proof of conceptLicensing Status:
This technology is available for licensingLicensing Potential:
This technology would be of interest to anyone involved in the development of carrier-based therapeutics, including:
•    Pharmaceutical companies.
•    Hospitals.
•    Medical research laboratories.
•    Educational institutions.

 

Computationally predicts potential ideal interaction points for the molecular chaperone heat shock protein-90 (Hsp90). Background:
Molecular chaperones assist in the folding of unfolded and misfolded polypeptides by stabilization of folding intermediates and prevention of protein misfolding and aggregation. Molecular chaperones are present in all organisms and are essential for cell survival. The chaperone heat shock protein-90 (Hsp90) controls the folding of client proteins important for tumorigenesis. Hsp90 facilitates the maturation of substrates (or clients) that are involved in many different cellular pathways. Hsp90 clients include, among others, kinases, transcription factors, steroid hormone receptors and E3 ubiquitin ligases. The development of Hsp90 ATP-competitive inhibitors has been limited partly because it results in the simultaneous blockage of all clients, ultimately causing antiapoptotic heat shock response.Technology Overview:  
This technology computationally predicts the most unstable regions on the native structures of clients c-Abl, c-Src, Cdk4, B-Raf and Glucocorticoid Receptor, as potential ideal interaction points with the Hsp90-system. This enables researchers to synthesize peptide mimics spanning these regions and confirm their interaction with partners of the Hsp90 complex (Hsp90, Cdc37 and Aha1) by Nuclear Magnetic Resonance (NMR). Designed non-naturally occurring peptides selectively disrupt the association of their respective clients with the Hsp90 machinery, leaving unrelated clients unperturbed and causing apoptosis in cancer cells. Overall, selective targeting of Hsp90 protein-protein interactions is achieved without causing indiscriminate degradation of all clients, setting the stage for the development of therapeutics based on specific chaperone:client perturbation.
 https://suny.technologypublisher.com/files/sites/adobestock_4870932151.jpegAdvantages:  
•    Enables the development of therapeutics based on Hsp90.
•    Avoids antiapoptotic heat shock response.  Applications:  
The primary application for this technology is the development of therapeutics based on Hsp90.  Intellectual Property Summary:
PCT Nationalized, including US2021/0214734 and EP4090679Stage of Development:
TRL 3 - Experimental proof of concept Licensing Status:
This technology is available for licensing.Licensing Potential:
This technology would be of interest to anyone involved in the development of therapeutics based on Hsp90, including:
•    Pharmaceutical manufactures.
•    Hospitals.
•    Medical laboratories.
•    Universities.

Background:
Platelet serotonin release assay (SRA) is a widely-used clinical assay for diagnosing heparin-induced thrombocytopenia (HIT), a life-threatening complication of heparin treatment. The current SRA procedure entails sending patient serum to a facility for testing by radioactive serotonin uptake/release or by mass spectrometry. Both assay methods require specialized equipment and trained personnel, with a turnaround time typically between three to seven days. Unfortunately, the mortality of HIT increases significantly with each passing day. As a result, quicker SRA turnaround time could save lives. Ideally, point-of-care facilities would obtain SRA results within hours, using inexpensive equipment and no special training to perform.Technology Overview:  
This technology is a luminescent biosensor that changes from green to blue in the presence of a target analyte. The biosensor consists of two molecules. The first is a specially designed green-to-blue color-changing luminescent protein (nLuc-AFF). The second is one or more short (20-50 nucleotide) DNA hairpins or DNA aptamers of novel design. These bind the target DNA sequence, RNA sequence, small molecule, or protein. Upon binding, the AP-1 sequence becomes exposed and activates the biosensor. The biosensor can be readily adapted to recognize different targets by modifying the DNA component, using existing online DNA design tools. The color change is visible and detection/quantification is via cell phone camera. https://suny.technologypublisher.com/files/sites/adobestock_446068375.jpegAdvantages:  
•    Produces results within hours.
•    Requires no special training or expensive equipment.
•    Can be easily adapted to recognize a variety of targets.
 Applications:  
•    Improved platelet SRA for diagnosing HIT.
•    Rapid detection of virus or other pathogen infection, such as coronavirus or cytomegalovirus.
•    Rapid detection of disease biomarkers such as microRNA, metabolites, or aberrant proteins.
 Intellectual Property Summary:
Know-how basedStage of Development:
TRL 3 - Experimental proof of concept Licensing Status:
This technology is available for licensing.Licensing Potential:
This technology would be of interest to anyone involved in the development of methods for detection of HIT and other conditions. These include:
•    Pharmaceutics companies.
•    Hospitals.
•    Medical research laboratories.
•    Universities.