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Description of Technology:

Cancer is one of the leading causes of death in United States and it is estimated that there will be more than half a million deaths caused by cancer in 2009.  A major drawback of the current chemotherapy-based therapeutics is the cytotoxic side-effects associated with them.  Thus there is a dire need to develop new therapeutic strategies with fewer side-effects.  Immunotherapy has taken a lead among the new therapeutic approaches.  Enhancing the innate immune response of an individual has been a key approach for the treatment against

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The National Institute on Drug Abuse's Medications Discovery Research Branch is seeking statements of capability or interest from parties interested in collaborative research to further develop, evaluate, or commercialize 4-phenylpiperazine derivatives as dopamine D3 selective ligands.

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The National Cancer Institute (NCI) seeks research co-development partners and/or licensees for viral peptide (CE1)-based therapeutics for HCC prevention and treatment.

Summary:

The National Cancer Institute (NCI) seeks licensees for matched patient-derived 3D Isocitrate Dehydrogenase (IDH)-mutant glioma cell lines, 403L and 403H, generated from the same patient before and after malignant transformation from WHO grade 2 to WHO grade 4 disease. This research material provides an opportunity to study IDH-mutant glioma progression, temozolomide-associated hypermutation, invasion, metabolism, and treatment resistance.

This technology involves the creation of monoclonal antibodies through hybridoma technology, specifically, hybridomas 3B6, 14B7, 2D3, 2G4, 1G3, 6H3, 6C5, and 3D12, which exhibit a high degree of reactivity with Bacillus anthracis protective antigen (PA). These monoclonal antibodies have shown great promise in the field of anthrax detection and diagnosis. Their exceptional specificity for Bacillus anthracis PA suggests their potential application in diagnostic devices.

Trispecific and trivalent binding proteins represent a breakthrough in the battle against HIV infection. These specialized proteins are engineered with four polypeptide chains forming three antigen binding sites, enabling precise targeting of HIV target proteins. Addressing the formidable challenges of HIV treatment, including the virus's high mutation rate and the persistence of viral reservoirs, these binding proteins offer a potential solution to breakthrough infections.

Researchers from the National Institute of Allergy and Infectious Diseases (NIAID) and the University of Maryland have unveiled a groundbreaking discovery, revealing the formation of a recombinant heterodimer known as p40-CD5L by combining two known proteins, p40 and CD5L. This heterodimer's significance lies in its ability to stimulate the production of interleukin-4 (IL-4) and interleukin-10 (IL-10) by T cells, which holds great promise for addressing conditions such as allergies, asthma, and tumor immunology.

The technology revolves around the discovery of SIRPα (Signal Regulatory Protein alpha) expression on CD8+ T cells as a novel biomarker for assessing T cell functionality during immune exhaustion, a state commonly induced by chronic infections and cancer. The unique expression profile of SIRPα on a subset of functional CD8+ T cells that retain cytotoxic capabilities despite an exhausted phenotype opens new avenues for therapeutic interventions.

Novel CD8+ T cell receptors (TCRs) isolated from elite HIV controllers show unprecedented affinity for conserved HIV epitopes, offering new avenues for direct immunotherapies and T cell engineering. These TCRs exhibit potential for cytotoxicity mediation against HIV-infected cells, with prospects for use in toxin-coupled treatments or as part of engineered T cell therapies. Collaborations, such as with Altor Biosciences, are enhancing these TCRs with proprietary molecules like IL-15, to bolster therapeutic efficacy.

The technology described pertains to the development of bispecific antibodies with enhanced ability to neutralize HIV-1. By structurally designing single chain fragment variable antibodies that join variable regions of multiple broadly neutralizing antibodies (bNAbs) with flexible linkers, the research has yielded a bispecific antibody that targets different epitopes on the HIV-1 envelope. The combination of VRC01—targeting the CD4 binding site—and PGT121—targeting the V3 glycan—has shown promising results.