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A β-lactoglobulin amyloid fibrils-poly(vinyl alcohol)-Ag nanoparticles (β-LAFs-PVA-AgNPs) hydrogel was prepared as a surface-enhanced Raman scattering (SERS) substrate based on poly(vinyl alcohol) (PVA) with adsorbent β-lactoglobulin amyloid fibrils (β-LAFs) structured into the network structure of the hydrogel using the immersion reduction method. Due to the high swelling and contraction properties of the hydrogel in different states and the "sieving" nature of its network cavities, small molecular target analytes can more easily enter the space-confined hydrogel and rapidly bind with the amide bonds of the protein structure. During the contraction process of the hydrogel, the target analytes are enriched, and the Ag nanoparticles (AgNPs) come closer together to form Raman "hot spots", generating stronger SERS signals. The SERS performance of this hydrogel was evaluated using thiram and ibuprofen as target molecules. The results showed high detection sensitivity with limits of 37.1 μg/L for thiram and 85.6 μg/L for ibuprofen, respectively, and the entire sample pretreatment and detection process is completed within 11 min. The substrate also demonstrated excellent selectivity, uniformity, stability, and reproducibility. When applied to detect thiram in fruits and vegetables and ibuprofen in herbal tea, the recovery rates ranged from 90.1% to 114.7%, with the relative standard deviations (RSDs) of 0.61% to 5.8%. The SERS results matched those from HPLC analysis. This method offers simple and rapid sample pretreatment, high sensitivity, strong adsorption capacity for organic pollutants, and good selectivity, making it a promising candidate for on-site rapid detection applications.
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http://dx.doi.org/10.1021/acs.analchem.5c02529 | DOI Listing |
Pharmacol Ther
September 2025
Department of Anesthesiology and Perioperative Medicine, Mayo Clinic, Rochester, MN 55902, USA; Department of Pharmacology and Experimental Therapeutics, Mayo Clinic, Rochester, MN 55902, USA.
Under physiological conditions, amyloid precursor protein (APP) is critically important for normal brain development, neurogenesis, neuronal survival, and synaptic signaling. Dyshomeostasis of APP increases deposition and accumulation of amyloid β (Aβ) in the brain parenchyma and cerebral blood vessels thereby leading to development of Alzheimer's disease and cerebral amyloid angiopathy. In this review, we critically examine existing literature supporting the concept that endothelial APP performs important vascular protective functions in the brain.
View Article and Find Full Text PDFInt J Biol Macromol
September 2025
Environmental Science and Engineering, Tianjin University, Tianjin, 300350, PR China.
Stable, treatment-resistant Cu complexes in practical wastewater are frequently neglected. Positively charged lysozyme amyloid fibrils (AF), however, exhibit unexplored potential for their adsorption. This study engineered an amyloid fibril-chitosan composite (AF-CS) xerogel and evaluated its adsorption performance in three systems: free Cu, Cu-Citrate binary, and Cu-EDTA binary.
View Article and Find Full Text PDFNeuropeptides
September 2025
Department of Physiology and Cell Biology, The National Institute for Biotechnology in the Negev, and the School of Brain Sciences and Cognition, Ben-Gurion University of the Negev, Beer-Sheva, Israel.
Despite extensive research into Alzheimer's disease (AD), few therapeutic strategies have successfully addressed its core pathology at the synaptic level. Small peptides represent a promising class of therapeutic agents capable of modulating key molecular pathways involved in amyloid toxicity, tau hyperphosphorylation, and synaptic degeneration. Their unique ability to cross biological barriers, interact with intracellular targets, and be modified for enhanced stability positions them as viable candidates for next-generation treatments targeting cognitive decline in AD.
View Article and Find Full Text PDFBiophys Chem
September 2025
Department of Biophysics, Faculty of Biological Sciences, Tarbiat Modares University, Tehran, Iran.
A comprehensive understanding of the molecular mechanism underlying the Liquid-Liquid Phase Separation (LLPS) pathway of LCD-TDP43 remains a challenge in the context of its neuropathogenesis. The primary driving force behind the TDP-43 LLPS is the interplay of hydrophobic interactions reinforced by aromatic residues. This study presents a novel, convenient, sensitive, and probe-free approach using excitation-emission matrix (EEM) fluorescence to monitor the microenvironment of aromatic residues and π-π stacking interactions during different stages of the LLPS pathway.
View Article and Find Full Text PDFSpectrochim Acta A Mol Biomol Spectrosc
August 2025
Department of Biochemistry and Biophysics, Stockholm University, Sweden. Electronic address:
Aggregation of the amyloid-β peptide (Aβ) characterises and probably causes Alzheimer's disease. While lipid-mediated Aβ aggregation has been extensively studied for the 40-residue variant Aβ40, the interaction of the 42-residue variant Aβ42 with membranes has received less attention. Our time-resolved infrared spectra demonstrate that Aβ42 oligomers preserve their β-sheet structure in aqueous solution also in a membrane-mimicking environment consisting of either 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine (POPC, zwitterionic) or 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'racglycerol) (POPG, anionic) vesicles.
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