Surface-enhanced Raman scattering (SERS) and surface-enhanced fluorescence (SEF) from individual plasmonic oligomers are investigated by confocal Raman micro-spectroscopy and time-resolved fluorescence microscopy coupled to steady state micro-spectroscopy. The nanoparticle (NP) oligomers are made of either ligand protected Au or Au@SiO2 core-shell colloidal NPs, which were assembled into ordered arrays by atomic force microscopy (AFM) nanoxerography. A strong dependence of the SERS emission on the polarization of incident light relative to the specific geometry of the plasmonic oligomer was observed. The SEF studies, performed on a large collection of NP oligomers of various known configurations showed interesting fluorophore decay rate modification and red-shift of the emission spectra. The experimental results are analyzed theoretically by employing finite-difference time-domain (FDTD) simulations on equivalent realistic structures, within the local density of optical states (LDOS) framework. The presented results, together with the proven potential of the LDOS approach as a useful common tool for analyzing both SERS and SEF effects further the general understanding of plasmon-related phenomena in nanoparticle oligomers.
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http://dx.doi.org/10.1039/c4nr05092d | DOI Listing |
Int J Mol Sci
December 2024
Laboratory of Pharmacodynamics and Pharmacokinetics, Istituto di Ricerche Farmacologiche Mario Negri IRCCS Via Mario Negri 2, 20156 Milan, Italy.
Amyloid-β1-42 (Aβ42) forms highly stable and insoluble fibrillar structures, representing the principal components of the amyloid plaques present in the brain of Alzheimer's disease (AD) patients. The involvement of Aβ42 in AD-associated neurodegeneration has also been demonstrated, in particular for smaller and soluble aggregates (oligomers). Based on these findings and on genetic evidence, Aβ42 aggregates are considered key players in the pathogenesis of AD and targets for novel therapies.
View Article and Find Full Text PDFCurr Res Food Sci
October 2024
Department of Biotechnology and Biosciences, University of Milano-Bicocca, Milano, Italy.
Neurodegenerative diseases are among the major challenges in modern medicine, due to the progressive aging of the world population. Among these, Parkinson's disease (PD) affects 10 million people worldwide and is associated with the aggregation of the presynaptic protein α-synuclein (α-syn). Here we use two different PD models, yeast cells and neuroblastoma cells overexpressing α-syn, to investigate the protective effect of an extract from the cocoa shell, which is a by-product of the roasting process of cocoa beans.
View Article and Find Full Text PDFMol Neurobiol
September 2024
Department of Neuroscience, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.
The most common cause of dementia among elderly people is Alzheimer's disease (AD). The typical symptom of AD is the decline of cognitive abilities, which is caused by loss of synaptic function. Amyloid-β (Aβ) oligomers play a significant role in the development of this synaptic dysfunction.
View Article and Find Full Text PDFBiotechnol Appl Biochem
September 2024
Institute of Biomedical Engineering, Boğaziçi University, Istanbul, Turkey.
Alpha-synuclein oligomers play a crucial role in the early diagnosis of Parkinson's disease (PD). In this study, a mercaptoundecanoic acid (MUA)-capped gold nanorod (GNR)-coated and chitosan (CH)-immobilized fiber optic probe has shown considerable sensitivity of its detection. The proposed U-shaped fiber optic biosensor based on localized surface plasmon resonance (LSPR) was applied to detect α-syn oligomer (OA) biomarker.
View Article and Find Full Text PDFAlzheimers Dement
October 2024
Department of Neurology, University Medical Center and the German Center for Neurodegenerative Diseases (DZNE), Georg-August University, Goettingen, Germany.
Introduction: Cellular prion protein (PrP) was implicated in amyloid beta (Aβ)-induced toxicity in Alzheimer's disease (AD), but the precise molecular mechanisms involved in this process are unclear.
Methods: Double transgenic mice were generated by crossing Prnp knockout (KO) with 5xFAD mice, and light-sheet microscopy was used for whole brain tissue analyses. PrP-overexpressing cells were developed for in vitro studies, and microscopy was used to assess co-localization of proteins of interest.
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