The Impacts Of Aluminum On The Abnormal Aggregation Of R3 Peptide Of Tau Protein And Its Mechanism

AD is a progressive mental deterioration manifested by memory loss, inability to calculate, visual-spatial disturbances, confusion and disorientation. Neurofibrillary tangles (NTFs) was one of its obvious pathological characteristics, composed by microtubule-associated protein Tau. Research showed that NTFs was highly relative to AD. Therefore Tau protein, as the component of NTFs, was considered a key point to the pathology of AD.It's reported that the R3 peptide of Tau protein was the most sensitive part for the abnormal aggregation which could aggregated at the minimum concentration compared with other peptides. In another way, the mechanism of R3 peptide abnormal aggregation was the access for discovering the cause of AD.Aluminum was a kind of environmental-abundant neurotoxin, being considered as one of the potential causes. Noteworthily, dialysis fluid of the AD patient contained Al at or above 0.5 μmol/L.Taking both the potential effect of Al and the key role of R3 peptide for AD into consideration, we carried out a systematic research on the impacts of Al on the aggregation of R3. A possible mechanism of the R3 peptide aggregation in the presence of Al was proposed based on the experiments data. Conclussions are summerized as below:1) Ths-Fluorescence method was applied to detect the aggregation of R3 peptide in the presence of Al, while the TEM method was used to observe the mophology of filaments aggregated by R3 peptide. Experiments confirmed the effect of Al on the R3 aggregation. The Ths-fluorescence results showed that the R3 peptide with Al³⁺ aggregated a little bit slower than the situation with heparin in the very beginning...