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METAL IONS BINDING TO AMYLOID-BETA AND NEUROPROTECTIVE NAP-LIKE PEPTIDES: MS, FT-IR AND AFM INVESTIGATIONS
Abstract
Alzheimer?s disease, the most common age-related dementia worldwide, is characterized by two pathologies: deposition of ?-amyloid plaque and neurofibrillary tangles of hyperphosphorylated tau. To this date, several factors, such as oxidative stress, metal ions, or genetic factors are associated with Alzheimer`s diseases, but there are still some question marks regarding: (i) how the misfolding and aggregation of A? occurs and which is the aggregation mechanism; (ii) how the metal ions binds to A? and how they initiate the aggregation process; (iii) can the aggregation process be reversed by using neuroprotective peptides? Nowadays, the research is also focused on finding and studying different compounds and peptides with neuroprotective role. Some scientific reports showed that peptides derived from activity-dependent neuroprotective protein (ADNP), such as NAP and D-SAL peptides are neuroprotective peptides. Moreover, there are some reports regarding the interaction of A? and NAP peptides with different metal ions (e.g. iron, copper, nickel, zinc, aluminum, etc.). Therefore, several ?-amyloid and anti-?-amyloid fragments have been synthesized by using solid phase peptide synthesis according to Boc/Bzl strategy. More precisely, the following amyloid and anti-amyloid peptides were synthesized: native A?1-16 peptide (H2N-DAEFRHDSGYEVHHQK-COONH2), Ala-A?1-16 peptide (H2N-DAEFRADSGYEVAAQK-COONH2), Ser-A?1-16 peptide (H2N-DAEFRSDSGYEVSSQK-COONH2), NAP peptide (H2N-NAPVSIPQ-COONH2), Ala-NAP (H2N-NAPVAIPQ-COONH2) and His-NAP (H2N-NAPVHIPQ-COONH2). Binding of metal ions to amyloid-? and anti- amyloid-? peptides was studied by mass spectrometry, infrared spectroscopy and atomic force microscopy. Our results reported here suggest that the affinity of metal ions to peptides is closely linked to the peptide sequence, the amino acid residues involved in metal binding and the type of metal ion used. The AFM investigations indicate that the more hydrophobic Ala-A?1-16 sequence in the presence of metal ions forms much easier fibrils than the native A?1-16 peptide.
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