Abstract
AbstractBackgroundOne of the common neurodegenerative disorders is the aggregation of Tau protein plays a major role in Alzheimer’s disease. Transmission metals ions such as Cu, Zn, and Fe are vital ingredients that must maintain homeostasis in the biological system. Tau Protein has four repeat peptide units (R1 R2 R3 R4) which may coordinate divalent copper ions to form neurofibrillary tangles (NFTs) and generate reactive oxygen species (ROS).The abnormal amount of Cu2+ accumulation in the intracellular environment, regulating the biological systems is not clearly understood.MethodThe main objective of this study was to evaluate the coordination of four R peptides to Cu2+ by MALDI‐MS‐TOF and determine the interaction of Cu2+ ions with peptides (R1 R2 R3 R4) of Tau protein in vitro. Also, their role in the formation of ROS with a natural reducing agent‐ ascorbate was probed.ResultAs the principal findings of this experiment, metal ion coordinated all 4 R peptides, via His and Cys residue including N terminal and amide groups. All the metallo‐peptide complexes were singly charged peaks, and observed even in the presence of ascorbate. R2 and R3 peptides formed the homodimers by disulfide bond formation. The metallo‐peptides were antioxidants and prooxidants depending on the conditions, indicating that a complex behavior may exist in the biological setting.ConclusionThis work indicates that metal ions interact with R peptides, which may mitigate ROS levels. The finding of this study is greatly beneficial for understanding the Tau protein behavior to develop a potential medication.
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