Abstract
Alzheimer’s disease (AD) is classified as an amyloid-related disease. Amyloid beta (Aβ) is a transmembrane protein known to play a major role in the pathogenesis of AD. These Aβ proteins can form ion channels or pores in the cell membrane. Studies have elucidated the structure of the transmembrane domain of Aβ ion channels. In addition, various studies have investigated substances that block or inhibit the formation of Aβ ion channels. Zinc ions are considered as potential inhibitors of AD. In this study, we focused on the transmembrane domain and some external domains of the Aβ protein (hAPP-TM), and solution-state NMR was used to confirm the effect on residues of the protein in the presence of zinc ions. In addition, we sought to confirm the structure and orientation of the protein in the presence of the bicelle using solid-state NMR.
Highlights
Neurodegenerative diseases are incurable and debilitating conditions that result in progressive degeneration and nerve cell death
We focused on the formation of the Aβ ion channel and demonstrated the ability of zinc ions to close the ion channel of the Aβ protein via structural changes in membrane proteins
We expressed a protein in E. coli with an amino acid sequence containing residues 692-723 of the transmembrane region of human amyloid precursor protein (APP)
Summary
Neurodegenerative diseases are incurable and debilitating conditions that result in progressive degeneration and nerve cell death. We focused on the formation of the Aβ ion channel and demonstrated the ability of zinc ions to close the ion channel of the Aβ protein via structural changes in membrane proteins. We expressed a protein in E. coli with an amino acid sequence containing residues 692-723 of the transmembrane region of human APP (hAPP-TM). Wheel pattern and the mechanism of hAPP-TM confirmed Both Aβ40 and Aβ42 contain a hydrophilic N-terminus that contains a metal protein was elucidated. We focused on the amino acid residues 692 and 723 (hAPP-TM), which have affinity for metal ions, including zinc ions, among the APPs [31]
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