This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Alzheimer's disease is a neurodegenerative ailment that affects predominantly the aged, and its impact is felt increasingly in ageing populations world-wide. There is much interest in finding cures to this debilitating disease through studying the disease mechanism and identifying promising targets. It is increasingly accepted that Alzheimer's disease occurs due to an increased production of a short peptide called Aa42, the aggregation of which is toxic to brain neurones and compromises neural function. The peptide arises through cleavage caused by proteins called secretases, of the amyloid precursor protein (APP) found on the cell surface. Plausible functional roles of the APP have been proposed and the relevant parts or domains of the APP identified. As some of these domains represent possible drug targets for treating Alzheimer's disease, it is crucial to determine the structures of the domains and their binding partners. By understanding how these domains bind to their ligands at a structural level, one can consider the search of suitable mimetics or modifications to these ligands. To this end a program of structure based drug design is currently under way in out laboratory with the known structures being screened in silico for target compounds. These target compounds will be soaked or co-crystallized with the domains and the binding structurally characterised.
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| Yang, Cheolhee; Choi, Minseo; Kim, Jong Goo et al. (2018) Protein Structural Dynamics of Wild-Type and Mutant Homodimeric Hemoglobin Studied by Time-Resolved X-Ray Solution Scattering. Int J Mol Sci 19: |
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| Yang, Xiaojing; Stojkovi?, Emina A; Ozarowski, Wesley B et al. (2015) Light Signaling Mechanism of Two Tandem Bacteriophytochromes. Structure 23:1179-89 |
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