Acid-Cleavable and Clickable Affinity Capture Probe

A Protein Capture Probe with High Sensitivity, Low Noise and Easy Release of the Target Protein Background: Identification of protein that binds a ligand is still a challenge. Probes must bind to the target protein with sufficient affinity and selectivity that allows isolation of the protein, without causing damage to the molecular structure of the protein-A typical strategy is to prepare a bi-functional probe, with one end containing the ligand and the other end containing a moiety which enables capture and isolation of the ligand-protein complex. Modification of the ligand can alter binding affinity and specificity. a better approach is to incorporate a small chemical "handle" onto the ligand to which the capture reagent can be covalently attached after binding to the receptor is complete. Technology Overview: This technology, developed by Dr. Nicole Sampson at Stony Brook University provides a capture probe with a cleavable linker that can be used with any ligand that has been modified with a small alkynyl group. . The capture reagent can be attached to the ligand once bound to the target protein using a simple chemical reaction, which then enables the capture reagent to be used to isolate a protein-ligand complex from a cellular mixture Once cleaved/released, the purified protein can be identified by standard mass spectrometric methods known in the art or further modified through the unmasked aldehyde. Advantages: Selectively removal of only the desired protein from the matrix. Increased stability, stable in many biological fluids. Applications: Research tool: compound identification, protein-protein interaction Intellectual Property Summary: US2014/0273010 Stage of Development: Licensing Potential: We seek to develop and commercialize, by an exclusive or non-exclusive license agreement and/or sponsored research, with a company active in the area Licensing Status: Available for License Additional Information: Lee, S. Org. Biomol. Chem. 2015, 13, 8445
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