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Current Topics in Peptide & Protein Research   Volumes    Volume 23 
Interactions of amyloid precursor protein intracellular domain (AICD) with copper and DNA fragment reveal conformational changes that trigger AD
D. Jagadeesh Kumar, M. Govindaraju, Priya Narayan, P. Ramasamy, H. G. Nagendra, K. S. Jagannatha Rao, K. R. K. Easwaran
Pages: 37 - 46
Number of pages: 10
Current Topics in Peptide & Protein Research
Volume 23 

Copyright © 2022 Research Trends. All rights reserved

Neurofibrillary tangles and Amyloid plaques are central to the progression of Alzheimer’s disease [AD]. It has been well substantiated that the Amyloid precursor protein is cleaved enzymatically at its C terminal end yielding the APP intracellular domain [AICD]. It has been shown that AICD is an intrinsically unstructured molecule involved in AD pathology and appears to be a potential candidate in understanding the complexity of this disease. However, the relevance of AICD mechanism in neurodegeneration is poorly understood. Recent evidences reveal that AICD is localized in the nucleus, and upon binding to DNA, gene expression appears to get altered, and this could be regarded as the third hallmark of AD. Reports have highlighted that higher concentrations of copper induces a neurotoxic effect, which could enhance the AD pathogenesis. Hence, our work using circular dichroism and computational studies focuses on the interactions of AICD with copper and DNA which indicates that AICD-Cu complex interacts with the DNA and triggers conformational perturbations leading to AD.
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