ANCUTA-VERONICA LUPAESCU, ION SANDU, BRINDUSA ALINA PETRE, LAURA ION, CATALINA-IONICA CIOBANU, GABI DROCHIOIU NAP NEUROPROTECTIVE PEPTIDE AND ITS ANALOGS: SIMULTANEOUSLY COPPER AND IRON BINDING AND REDUCTION Neurodegenerative diseases, including Alzheimer disease, involve mechanisms such as protein aggregation, free radical generation and oxidative stress. Transition metals such as copper and iron were linked to neurodegenerative pathology. Their pathogenic role consists in generating different reactive oxygen species and damaging tissues or cells through the Fenton reaction. Abnormal metabolism of copper and iron can lead to several chronic pathogenesis. NAP is a small active fragment of activity-dependent neuroprotective protein essential for brain formation. NAP peptide showed neuroprotective proprieties against toxicity induced by the â-amyloid peptide, N-methyl-D-aspartate, electrical blockade, the envelope protein of the AIDS virus, dopamine, H2O2, and nutrient starvation in cell culture. Therefore, we investigated here the interaction of Cu2+ and Fe3+ ions with the NAP neuroprotective peptide and its analogs. With MALDI-ToF mass spectrometry, the formation of reduced metal-peptide complexes and the metal chelating properties of NAP-like neuroprotective peptides were highlighted.
Keywords: NAP peptide, neuroprotection, copper, iron, MALDI-ToF MS