Relevant bibliographies by topics / Amyloid Protein-Nanoparticle

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Academic literature on the topic 'Amyloid Protein-Nanoparticle'

Author: Grafiati
Published: 7 September 2023

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Journal articles on the topic "Amyloid Protein-Nanoparticle"

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Wang, Bo, Emily H. Pilkington, Yunxiang Sun, Thomas P. Davis, Pu Chun Ke, and Feng Ding. "Modulating protein amyloid aggregation with nanomaterials." Environmental Science: Nano 4, no. 9 (2017): 1772–83. http://dx.doi.org/10.1039/c7en00436b.

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Radic, Slaven, Thomas P. Davis, Pu Chun Ke, and Feng Ding. "Contrasting effects of nanoparticle–protein attraction on amyloid aggregation." RSC Advances 5, no. 127 (2015): 105489–98. http://dx.doi.org/10.1039/c5ra20182a.

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D’Onofrio, Mariapina, Francesca Munari, and Michael Assfalg. "Alpha-Synuclein—Nanoparticle Interactions: Understanding, Controlling and Exploiting Conformational Plasticity." Molecules 25, no. 23 (November 29, 2020): 5625. http://dx.doi.org/10.3390/molecules25235625.

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Alpha-synuclein (αS) is an extensively studied protein due to its involvement in a group of neurodegenerative disorders, including Parkinson′s disease, and its documented ability to undergo aberrant self-aggregation resulting in the formation of amyloid-like fibrils. In dilute solution, the protein is intrinsically disordered but can adopt multiple alternative conformations under given conditions, such as upon adsorption to nanoscale surfaces. The study of αS-nanoparticle interactions allows us to better understand the behavior of the protein and provides the basis for developing systems capable of mitigating the formation of toxic aggregates as well as for designing hybrid nanomaterials with novel functionalities for applications in various research areas. In this review, we summarize current progress on αS-nanoparticle interactions with an emphasis on the conformational plasticity of the biomolecule.
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Paramasivam, Santhosh, Kavita Kundal, and Nandini Sarkar. "Human Serum Albumin Aggregation and its Modulation Using Nanoparticles: A Review." Protein & Peptide Letters 29, no. 1 (January 2022): 11–21. http://dx.doi.org/10.2174/0929866528666211125104600.

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: Amyloid fibrils are highly stable protein fibrillar aggregates believed to be involved in various neurodegenerative diseases, which include Alzheimer’s disease, Parkinson’s disease, and prion diseases. Inhibiting the aggregation process is a potential strategy to prevent diseases caused by amyloid formation. In this regard, nanoparticles have emerged as promising candidates owing to their unique physical/chemical properties of small size, large surface area, biocompatibility, biodegradability, non-toxicity, and ease of functionalization. Human Serum Albumin (HSA) is a soluble multidomain monomeric protein that interacts with various ligands and hormones, aiding in their transport, distribution, metabolism in the circulatory system, and also plays a vital role in extracellular fluid volume stabilization. Under certain in vitro conditions, HSA has been reported to undergo conformational changes leading to fibril formation and hence acts as a suitable model for studying amyloidogenesis. In this review, we have explored the effects of various nanoparticles on HSA aggregation and their mechanism of action. The study will throw light on the mechanistic details of nanoparticle-mediated amyloid modulation, which will help in the development of effective therapeutics against amyloidosis.
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Wang, Jie, Yonghai Feng, Xiaohua Tian, Chenglong Li, and Lei Liu. "Disassembling and degradation of amyloid protein aggregates based on gold nanoparticle-modified g-C3N4." Colloids and Surfaces B: Biointerfaces 192 (August 2020): 111051. http://dx.doi.org/10.1016/j.colsurfb.2020.111051.

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Hess, Kayla A., Nathan J. Spear, Sophia A. Vogelsang, Janet E. Macdonald, and Lauren E. Buchanan. "Determining the impact of gold nanoparticles on amyloid aggregation with 2D IR spectroscopy." Journal of Chemical Physics 158, no. 9 (March 7, 2023): 091101. http://dx.doi.org/10.1063/5.0136376.

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As nanomaterials become more prevalent in both industry and medicine, it is crucial to fully understand their health risks. One area of concern is the interaction of nanoparticles with proteins, including their ability to modulate the uncontrolled aggregation of amyloid proteins associated with diseases, such as Alzheimer’s disease and type II diabetes, and potentially extend the lifetime of cytotoxic soluble oligomers. This work demonstrates that two-dimensional infrared spectroscopy and 13C18O isotope labeling can be used to follow the aggregation of human islet amyloid polypeptide (hIAPP) in the presence of gold nanoparticles (AuNPs) with single-residue structural resolution. 60 nm AuNPs were found to inhibit hIAPP, tripling the aggregation time. Furthermore, calculating the actual transition dipole strength of the backbone amide I’ mode reveals that hIAPP forms a more ordered aggregate structure in the presence of AuNPs. Ultimately, such studies can provide insight into how mechanisms of amyloid aggregation are altered in the presence of nanoparticles, furthering our understanding of protein–nanoparticle interactions.
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Windheim, Joseph, Laura Colombo, Nora C. Battajni, Luca Russo, Alfredo Cagnotto, Luisa Diomede, Paolo Bigini, et al. "Micro- and Nanoplastics’ Effects on Protein Folding and Amyloidosis." International Journal of Molecular Sciences 23, no. 18 (September 7, 2022): 10329. http://dx.doi.org/10.3390/ijms231810329.

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A significant portion of the world’s plastic is not properly disposed of and, through various processes, is degraded into microscopic particles termed micro- and nanoplastics. Marine and terrestrial faunae, including humans, inevitably get in contact and may inhale and ingest these microscopic plastics which can deposit throughout the body, potentially altering cellular and molecular functions in the nervous and other systems. For instance, at the cellular level, studies in animal models have shown that plastic particles can cross the blood–brain barrier and interact with neurons, and thus affect cognition. At the molecular level, plastics may specifically influence the folding of proteins, induce the formation of aberrant amyloid proteins, and therefore potentially trigger the development of systemic and local amyloidosis. In this review, we discuss the general issue of plastic micro- and nanoparticle generation, with a focus on their effects on protein folding, misfolding, and their possible clinical implications.
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Lizoń, Anna, Magdalena Wytrwal-Sarna, Marta Gajewska, and Ryszard Drożdż. "Silver Nanoparticle-Based Assay for the Detection of Immunoglobulin Free Light Chains." Materials 12, no. 18 (September 15, 2019): 2981. http://dx.doi.org/10.3390/ma12182981.

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There is a wide spectrum of malignant diseases that are connected with the clonal proliferation of plasma cells, which cause the production of complete immunoglobulins or their fragments (heavy or light immunoglobulin chains). These proteins may accumulate in tissues, leading to end organ damage. The quantitative determination of immunoglobulin free light chains (FLCs) is considered to be the gold standard in the detection and treatment of multiple myeloma (MM) and amyloid light-chain (AL) amyloidosis. In this study, a silver nanoparticle-based diagnostic tool for the quantitation of FLCs is presented. The optimal test conditions were achieved when a metal nanoparticle (MNP) was covered with 10 particles of an antibody and conjugated by 5–50 protein antigen particles (FLCs). The formation of the second antigen protein corona was accompanied by noticeable changes in the surface plasmon resonance spectra of the silver nanoparticles (AgNPs), which coincided with an increase of the hydrodynamic diameter and increase in the zeta potential, as demonstrated by dynamic light scattering (DLS). A decrease of repulsion forces and the formation of antigen–antibody bridges resulted in the agglutination of AgNPs, as demonstrated by transmission electron microscopy and the direct formation of AgNP aggregates. Antigen-conjugated AgNPs clusters were also found by direct observation using green laser light scattering. The parameters of the specific immunochemical aggregation process consistent with the sizes of AgNPs and the protein particles that coat them were confirmed by four physical methods, yielding complementary data concerning a clinically useful AgNPs aggregation test.
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Coelho, Carina Marques, Lia Pereira, Pamela Teubig, Pedro Santos, Filipa Mendes, Sílvia Viñals, Daniel Galaviz, and Federico Herrera. "Radiation as a Tool against Neurodegeneration—A Potential Treatment for Amyloidosis in the Central Nervous System." International Journal of Molecular Sciences 23, no. 20 (October 14, 2022): 12265. http://dx.doi.org/10.3390/ijms232012265.

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Radiotherapy (RT) is a relatively safe and established treatment for cancer, where the goal is to kill tumoral cells with the lowest toxicity to healthy tissues. Using it for disorders involving cell loss is counterintuitive. However, ionizing radiation has a hormetic nature: it can have deleterious or beneficial effects depending on how it is applied. Current evidence indicates that radiation could be a promising treatment for neurodegenerative disorders involving protein misfolding and amyloidogenesis, such as Alzheimer’s or Parkinson’s diseases. Low-dose RT can trigger antioxidant, anti-inflammatory and tissue regeneration responses. RT has been used to treat peripheral amyloidosis, which is very similar to other neurodegenerative disorders from a molecular perspective. Ionizing radiation prevents amyloid formation and other hallmarks in cell cultures, animal models and pilot clinical trials. Although some hypotheses have been formulated, the mechanism of action of RT on systemic amyloid deposits is still unclear, and uncertainty remains regarding its impact in the central nervous system. However, new RT modalities such as low-dose RT, FLASH, proton therapy or nanoparticle-enhanced RT could increase biological effects while reducing toxicity. Current evidence indicates that the potential of RT to treat neurodegeneration should be further explored.
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Morris, Daniel C., Anja K. Jaehne, Michael Chopp, Zhanggang Zhang, Laila Poisson, Yalei Chen, Indrani Datta, and Emanuel P. Rivers. "Proteomic Profiles of Exosomes of Septic Patients Presenting to the Emergency Department Compared to Healthy Controls." Journal of Clinical Medicine 9, no. 9 (September 11, 2020): 2930. http://dx.doi.org/10.3390/jcm9092930.

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Background: Septic Emergency Department (ED) patients provide a unique opportunity to investigate early sepsis. Recent work focuses on exosomes, nanoparticle-sized lipid vesicles (30–130 nm) that are released into the bloodstream to transfer its contents (RNA, miRNA, DNA, protein) to other cells. Little is known about how early changes related to exosomes may contribute to the dysregulated inflammatory septic response that leads to multi-organ dysfunction. We aimed to evaluate proteomic profiles of plasma derived exosomes obtained from septic ED patients and healthy controls. Methods: This is a prospective observational pilot study evaluating a plasma proteomic exosome profile at an urban tertiary care hospital ED using a single venipuncture blood draw, collecting 40 cc Ethylenediaminetetraacetic acid (EDTA) blood. Measurements: We recruited seven patients in the ED within 6 h of their presentation and five healthy controls. Plasma exosomes were isolated using the Invitrogen Total Exosome Isolation Kit. Exosome proteomic profiles were analyzed using fusion mass spectroscopy and Proteome Discoverer. Principal component analysis (PCA) and differential expression analysis (DEA) for sepsis versus control was performed. Results: PCA of 261 proteins demonstrated septic patients and healthy controls were distributed in two groups. DEA revealed that 62 (23.8%) proteins differed between the exosomes of septic patients and healthy controls, p-value < 0.05. Adjustments using the False Discovery Rate (FDR) showed 23 proteins remained significantly different (FDR < 0.05) between sepsis and controls. Septic patients and controls were classified into two distinct groups by hierarchical clustering using the 62 nominally DE proteins. After adjustment multiple comparisons, three acute phase proteins remained significantly different between patients and controls: Serum amyloid A-1, C-reactive protein and Serum Amyloid A-2. Inflammatory response proteins immunoglobulin heavy constant Δ and Fc-fragment of IgG binding protein were increased. Conclusion: Exosome proteomic profiles of septic ED patients differ from their healthy counterparts with regard to acute phase response and inflammation.
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Dissertations / Theses on the topic "Amyloid Protein-Nanoparticle"

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Dyne, Eric D. "Magnetic Nanoparticle Hyperthermia-Mediated Clearance of Beta-amyloid Plaques: Implications in the Treatment of Alzheimer’s Disease." Kent State University / OhioLINK, 2021. http://rave.ohiolink.edu/etdc/view?acc_num=kent1618706341759415.

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Frame, Nicholas. "The structural basis for lipid interactions of serum amyloid A." Thesis, 2019. https://hdl.handle.net/2144/38578.

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Serum amyloid A (SAA) is a small, evolutionarily well-conserved, acute-phase protein best known as the protein precursor for amyloid A amyloidosis. During acute injury, infection, or inflammation, SAA plasma concentration rapidly rises 1000-fold, but the benefit of this dramatic increase is unclear. SAA functions in the innate immune response, cell signaling, and lipid homeostasis. Most SAA circulates on plasma high-density lipoproteins (HDL), where it reroutes HDL for lipid recycling. The aim of this dissertation is to provide a structural basis for understanding SAA-lipid interactions and to elucidate the structure-function relationship in this ancient protein. SAA is an intrinsically disordered protein that acquires ~50% helical structure when bound to lipids, and is ~80% helical in three available atomic-resolution x-ray crystal structures. We took advantage of these crystal structures of lipid-free SAA to propose the binding site for various lipids, including lipids in HDL. We postulated that SAA, as a monomer, binds lipids via two amphipathic helices, h1 and h3, that form a concave hydrophobic surface, and that the curvature of this surface defines the binding preference of SAA for HDL versus larger lipoproteins. Next, we used murine SAA1.1 and a membrane-mimicking model phospholipid, palmitoyl-oleoyl phosphocholine (POPC), to reconstitute SAA-lipid complexes and characterize their overall structure, stability and stoichiometry using an array of spectroscopic, electron microscopic, and biochemical methods. We observed preferential formation of ~10 nm particles that mimic HDL size, accompanied by the α-helical folding. To probe the local protein conformation and dynamics in these SAA-POPC particles, we used hydrogen-deuterium exchange mass spectrometry. Analysis of the amount and the kinetics of deuterium uptake clearly established h1 and h3 as the lipid-binding site. Moreover, we determined that SAA binding to lipid follows a mixed model that combines induced fit, promoting α-folding in h3, with conformational selection, stabilizing pre-existing conformations in h1 and around the h2-h3 linker. Taken together, our results provided the structural basis necessary for understanding SAA-lipid interactions, which are central to beneficial functions of SAA as a housekeeping molecule, and to its misfolding in amyloid. This research sets the stage for understanding SAA interactions with its numerous other functional ligands.
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Book chapters on the topic "Amyloid Protein-Nanoparticle"

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Zhang, Genyi, Deepak Bhopatkar, Bruce R. Hamaker, and Osvaldo H. Campanella. "Self-assembly of amylose, protein, and lipid as a nanoparticle carrier of hydrophobic small molecules." In Nanotechnology and Functional Foods, 263–71. Chichester, UK: John Wiley & Sons, Ltd, 2015. http://dx.doi.org/10.1002/9781118462157.ch16.

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