A5078252196- Prion Diseases and Protein Misfolding
- Alzheimer's disease research and treatments
- Trace Elements in Health
- Distributed and Parallel Computing Systems
- Organic Chemistry Cycloaddition Reactions
- Molecular spectroscopy and chirality
- Photochemistry and Electron Transfer Studies
- Crystallography and molecular interactions
- Inorganic and Organometallic Chemistry
- Peer-to-Peer Network Technologies
- Molecular Spectroscopy and Structure
- Analytical Chemistry and Chromatography
- Advanced Software Engineering Methodologies
- Free Radicals and Antioxidants
- Protein Structure and Dynamics
- Distributed systems and fault tolerance
- Nonlinear Optical Materials Research
- Structural and Chemical Analysis of Organic and Inorganic Compounds
- Advanced Chemical Physics Studies
- Multi-Agent Systems and Negotiation
- Computational Drug Discovery Methods
- Enzyme Structure and Function
- Metal complexes synthesis and properties
- Synthesis and Reactivity of Sulfur-Containing Compounds
- Crystal structures of chemical compounds
National Research Council
2006-2025
Institute of Crystallography
2019-2025
Institute of Biostructure and Bioimaging
2011-2020
University of Catania
2009-2019
University of Calabria
2017
University of Reggio Calabria
1988-2015
National Academies of Sciences, Engineering, and Medicine
2013
University of Messina
2009
Institute for Chemical and Physical Processes
2009
Institute of Nanostructured Materials
2009
The 42-aa-long β-amyloid protein—Aβ 1-42 —is thought to play a central role in the pathogenesis of Alzheimer's disease (AD) (Walsh and Selkoe, 2007). Data from AD brain (Shankar et al., 2008), transgenic APP (amyloid precursor protein)-overexpressing mice (Lesné 2006), neuronal cultures treated with synthetic Aβ peptides (Lambert 1998) indicate that self-association monomers into soluble oligomers is required for neurotoxicity. function monomeric unknown. evidence present CSF normal...
A 31-mer polypeptide, which encompasses residues 84-114 of human prion protein HuPrP(84-114) and contains three histidyl residues, namely one from the octarepeat (His85) two outside region (His96 His111), its mutants with HuPrP(84-114)His85Ala, His96Ala, HuPrP(84-114)His111Ala HuPrP(91-115) have been synthesised their Cu2+ complexes studied by potentiometric spectroscopic (UV/Vis, CD, EPR, ESI-MS) techniques. The results revealed a high Cu2+-binding affinity all peptides, studies made it...
The N-terminal octapeptide repeat region of human prion protein (PrPc) is known to bind Cu(II). To investigate the binding modes copper in PrPc, an Ac-PHGGGWGQ-NH2 (1), which corresponds octa-repeat sequence, and a tetrapeptide Ac-HGGG-NH2 (2) have been synthesised. copper(II) complexes formed with 1 2 studied by circular dichroism (CD) electron spin resonance (ESR) spectroscopy. Both peptides form 1:1 Cu(II) at neutral basic pH. CD, ESR visible absorption spectra suggest similar...
Copper(II) complexes of the neurotoxic peptide fragments human and chicken prion proteins were studied by potentiometric, UV−vis, CD, EPR spectroscopic ESI-MS methods. The peptides included terminally blocked native scrambled sequences HuPrP106−126 (HuPrPAc106−126NH2 ScrHuPrPAc106−126NH2) also nona- tetrapeptide both (HuPrPAc106−114NH2, ChPrPAc119−127NH2, HuPrPAc109−112NH2, ChPrPAc122−125NH2). histidyl imidazole-N donor atoms found to be major copper(II) binding sites all peptides; 3N 4N...
Alzheimer's disease (AD) is becoming a rapidly growing health problem, as it one of the main causes dementia in elderly. Interestingly, copper(II) (together with zinc and iron) ions are accumulated amyloid deposits, suggesting that metal binding to Aβ could be involved AD pathogenesis. In Aβ, believed occur within N-terminal region encompassing amino acid residues 1−16. this work, potentiometric, spectroscopic (UV−vis, circular dichroism, electron paramagnetic resonance), electrospray...
Abstract Accumulation of neurotoxic amyloid‐β peptide (Aβ) and alteration metal homeostasis (metallostasis) in the brain are two main factors that have been very often associated with neurodegenerative diseases, such as Alzheimer’s disease (AD). Aβ is constantly produced from amyloidprecursor‐protein APP precursor immediately catabolized under normal conditions, whereas dysmetabolism and/or ions seems to lead a pathological deposition. Although insulin‐degrading enzyme (IDE) metalloprotease...
Complex formation processes between the 39-mer residue peptide fragment of human prion protein, HuPrP(76−114), and copper(II) ions have been studied by potentiometric, UV−vis, circular dichroism (CD), electron paramagnetic resonance, electrospray ionization mass spectrometry methods. This consists 39 amino acid residues contains two histidines (His77 His85) belonging to octarepeat domain (His96 His111) outside this domain. It was found that HuPrP(76−114) is able bind 4 equiv metal all...
Aggregation of the amyloid β-peptide (Aβ) into insoluble fibrils is a key pathological event in Alzheimer's Disease (AD). There now compelling evidence that metal binding to Aβ involved AD pathogenesis. The amino acid region 1-16 widely considered as domain Aβ. In this work, we used combined potentiometric, NMR, and electrospray ionization mass spectrometry (ESI-MS) approach study zinc(II) new polyethylene glycol (PEG)-conjugated peptide fragment encompassing sequence (Aβ(1-16)PEG). Our...
Amylin is a 37-residue peptide hormone produced by the islet β-cells of pancreas and formation amylin aggregates strongly associated with β-cell degeneration in type 2 diabetes, as demonstrated more than 95% patients exhibiting amyloid upon autopsy. It widely recognized that metal ions such copper(II) have been implicated aggregation process amyloidogenic peptides Aβ α-synuclein there evidence self-assembly also largely affected copper(II). For this reason, work, role has investigated...
The largest part of tau secreted from AD nerve terminals and released in cerebral spinal fluid (CSF) is C-terminally truncated, soluble unaggregated supporting potential extracellular role(s) NH
Abstract Mitochondrial porin or VDAC (voltage‐dependent anion‐selective channel) is the most abundant protein in mitochondrial outer membrane. The structure of has been predicted to be a transmembrane β‐barrel with an α‐helix at N terminus. It matter debate as whether this putative plays structural role component pore walls function activity. We have synthesised human VDAC1 (HVDAC1) N‐terminal peptide Ac‐AVPPTYADLGKSARDVFTK‐NH 2 ( Prn2 – 20 ) and determined its by CD NMR spectroscopy....
The effects of thermal treatment in the range 25−200 °C Zn/Al (ratio 2:1) synthetic hydrotalcites having chloride and carbonate as interlayer anions, formula [Zn0.65Al0.35(OH)2]Cl0.35·0.35H2O (I) [Zn0.65Al0.35(OH)2](CO3)0.175·0.69H2O (II), were studied using an integrated X-ray powder diffraction (XRPD)−molecular dynamics (MD) approach. main novelty this study consists calculating XRPD pattern with several MD structure models selected series instead a single structure. This was needed to...
Due to their altered metabolism cancer cells are more sensitive proteasome inhibition or changes of copper levels than normal cells. Thus, the development complexes endowed with features has emerged as a promising anticancer strategy. However, limited information is available about exact mechanism by which inhibits proteasome. Here we show that Cu(II) ions simultaneously inhibit three peptidase activities isolated 20S proteasomes potencies (IC50) in micromolar range. ions, cell-free...
ß-amyloid (Aß1-42) is produced by proteolytic cleavage of the transmembrane type-1 protein, amyloid precursor protein. Under pathological conditions, Aß1-42self-aggregates into oligomers, which cause synaptic dysfunction and neuronal loss, are considered culprit Alzheimer's disease (AD). However, Aß1-42 mainly monomeric at physiological concentrations, precise role in function largely unknown. We report that monomer activates insulin-like growth factor receptors enhances glucose uptake...