Elucidating the structure
These new structural insights into SARM1 are expected to facilitate advances in drug design for diseases such as multiple sclerosis, amyotrophic lateral sclerosis, and peripheral neuropathies. Bostjan Kobe of The University of Queensland, with Disarm scientists, has described the crystal structure of two important protein domains of SARM1, specifically the sterile alpha motif (SAM) and the toll/interleukin-1 receptor (TIR) domains.
This advance makes possible the use of sophisticated computational tools to accelerate drug discovery via structure-based drug design, with far-reaching implications for drug development in neurodegenerative diseases.
By inhibiting the SARM1 protein, identified by the company’s scientific founders as the central driver of axonal degeneration, these therapeutics may prevent the loss of axons in chronic and acute diseases of the central, ocular, and peripheral nervous systems.
For a broad range of diseases including multiple sclerosis, amyotrophic lateral sclerosis, glaucoma, and peripheral neuropathies, the therapeutic goal is to prevent further degeneration, stabilize disease, and allow for functional recovery.
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The crystal structures of both α- and β-Au Se consist of repeating units of a linearly bonded Au in Au Se which was not detected using XPS.
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