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The nature of bosonic excitations in disordered materials has remained elusive due to the difficulties in defining key concepts such as quasi-particles in the presence of disorder. We report on an experimental observation of phonon-polaritons in glasses, including a prominent boson peak (BP), i.e., excess of THz modes over the Debye law. A theoretical framework based on the concept of diffusons is developed to describe the broadening linewidth of the polariton due to disorder-induced scattering. It is shown here for the first time that the BP frequency and the Ioffe–Regel (IR) crossover frequency of the polariton collapse onto the same power-law decay with the diffusivity of the bosonic excitation. This analysis dismisses the hypothesis of the BP being caused by a relic of the van Hove singularity. The presented framework establishes a new methodology to analyze bosonic excitations in amorphous media, well beyond the traditional case of acoustic phonons, and establishes the IR crossover as the fundamental physical mechanism behind the BP. [ABSTRACT FROM AUTHOR]

α-Synuclein (αS), dopamine (DA), and iron have a crucial role in the etiology of Parkinson's disease. The present study aims to investigate the interplay between these factors by analyzing the DA/iron interaction and how it is affected by the presence of the C-terminal fragment of αS (Ac-αS119–132) that represents the iron-binding domain. At high DA:Fe molar ratios, the formation of the [FeIII(DA)2]– complex prevents the interaction with αS peptides, whereas, at lower DA:Fe molar ratios, the peptide is able to compete with one of the two coordinated DA molecules. This interaction is also confirmed by HPLC-MS analysis of the post-translational modifications of the peptide, where oxidized αS is observed through an inner-sphere mechanism. Moreover, the presence of phosphate groups in Ser129 (Ac-αSpS119–132) and both Ser129 and Tyr125 (Ac-αSpYpS119–132) increases the affinity for iron(III) and decreases the DA oxidation rate, suggesting that this post-translational modification may assume a crucial role for the αS aggregation process. Finally, αS interaction with cellular membranes is another key aspect for αS physiology. Our data show that the presence of a membrane-like environment induced an enhanced peptide effect over both the DA oxidation and the [FeIII(DA)2]– complex formation and decomposition. [ABSTRACT FROM AUTHOR]

Neuromelanins are compounds accumulating in neurons of human and animal brain during aging, with neurons of substantia nigra and locus coeruleus having the highest levels of neuromelanins. These compounds have melanic, lipid, peptide, and inorganic components and are contained inside special autolysosomes. Neuromelanins can participate in neuroprotective or toxic processes occurring in Parkinson's disease according to cellular environment. Their synthesis depends on the concentration of cytosolic catechols and is a protective process since it prevents the toxic accumulation of catechols‐derived reactive compounds. Neuromelanins can be neuroprotective also by binding reactive/toxic metals to produce stable and non‐toxic complexes. Extraneuronal neuromelanin released by dying dopamine neurons in Parkinson's disease activates microglia which generate reactive oxygen species, reactive nitrogen species, and proinflammatory molecules, thus producing still neuroinflammation and neuronal death. Synthetic neuromelanins have been prepared with melanic, protein structure, and metal content closely mimicking the natural brain pigment, and these models are also able to activate microglia. Neuromelanins have different structure, synthesis, cellular/subcellular distribution, and role than melanins of hair, skin, and other tissues. The main common aspect between brain neuromelanin and peripheral melanin is the presence of eumelanin and/or pheomelanin moieties in their structure. [ABSTRACT FROM AUTHOR]

Water‐soluble melanin‐protein‐Fe/Cu conjugates derived from norepinephrine and fibrillar β‐lactoglobulin are reliable models for neuromelanin (NM) of human brain locus coeruleus. Both iron and copper promote catecholamine oxidation and exhibit strong tendency to remain coupled in oligonuclear aggregates. The Fe‐Cu clusters are EPR silent and affect the 1H NMR spectra of the conjugates through a specific sequence of signals. Derivatives containing only Fe or Cu exhibit different NMR patterns. The EPR spectra show weak signals of paramagnetic FeIII in conjugates containing Fe or mixed Fe‐Cu sites due to small amounts of mononuclear centers. The latter derivatives exhibit EPR signals for isolated CuII centers. These features parallel the EPR behavior of NM from locus coeruleus. The spectral data indicate that FeIII is bound to the melanic fraction, whereas CuII is bound on the protein fibrils, suggesting that the Fe‐Cu clusters occur at the interface between the two components of the synthetic NMs. [ABSTRACT FROM AUTHOR]

The comparative studies of binding of NO and CO to chelated protoheme-L-histidine methyl ester (HM-H), protoheme-glycyl-L-histidine methyl ester (HM-Gh), and free protoheme (HM) is reported.