Journal ArticleDOI
Effect of Fe(3)O(4) magnetic nanoparticles on lysozyme amyloid aggregation.
Andrea Bellova,Eva Bystrenova,Martina Koneracka,Peter Kopcansky,Francesco Valle,Natália Tomašovičová,Milan Timko,Jaroslava Bagelova,Fabio Biscarini,Zuzana Gazova +9 more
TLDR
It is found that magnetic Fe(3)O(4) nanoparticles are able to interact with lysozyme amyloids in vitro leading to a reduction of the amyloid aggregates, thus promoting depolymerization and their non-risk exploitation in nanomedicine and nanodiagnostics.Abstract:
Peptide amyloid aggregation is a hallmark of several human pathologies termed amyloid diseases. We have investigated the effect of electrostatically stabilized magnetic nanoparticles of Fe(3)O(4) on the amyloid aggregation of lysozyme, as a prototypical amyloidogenic protein. Thioflavin T fluorescence assay and atomic force microscopy were used for monitoring the inhibiting and disassembly activity of magnetic nanoparticles of Fe(3)O(4). We have found that magnetic Fe(3)O(4) nanoparticles are able to interact with lysozyme amyloids in vitro leading to a reduction of the amyloid aggregates, thus promoting depolymerization; the studied nanoparticles also inhibit lysozyme amyloid aggregation. The ability to inhibit lysozyme amyloid formation and promote lysozyme amyloid disassembly exhibit concentration-dependent characteristics with IC50 = 0.65 mg ml(-1) and DC50 = 0.16 mg ml(-1) indicating that nanoparticles interfere with lysozyme aggregation already at stoichiometric concentrations. These features make Fe(3)O(4) nanoparticles of potential interest as therapeutic agents against amyloid diseases and their non-risk exploitation in nanomedicine and nanodiagnostics.read more
Citations
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Journal ArticleDOI
Potential toxicity of superparamagnetic iron oxide nanoparticles (SPION)
TL;DR: Current studies are reviewed and discussed how SPION, with or without different surface coating, may cause cellular perturbations including modulation of actin cytoskeleton, alteration in gene expression profiles, disturbance in iron homeostasis and altered cellular responses such as activation of signalling pathways and impairment of cell cycle regulation.
Journal ArticleDOI
Antimicrobial activity of iron oxide nanoparticle upon modulation of nanoparticle-bacteria interface
Manoranjan Arakha,Sweta Pal,Devyani Samantarrai,Tapan Kumar Panigrahi,Bairagi C. Mallick,Krishna Pramanik,Bibekanand Mallick,Suman Jha +7 more
TL;DR: The data indicated that the chitosan coating of IONP result in interface that enhances ROS production, hence the antimicrobial activity.
Journal ArticleDOI
Superparamagnetic Iron Oxide Nanoparticles—Current and Prospective Medical Applications
Joanna Dulińska-Litewka,Agnieszka Łazarczyk,Przemysław Hałubiec,Oskar Szafrański,Karolina Karnas,Anna Karewicz +5 more
TL;DR: The main goal of this paper is to present the basic properties of SPIONs, to discuss their current role in medicine, and to review their applications in order to inspire future developments of new, improved SPION systems.
Journal ArticleDOI
Synthesis and bio-functionalization of magnetic nanoparticles for medical diagnosis and treatment
TL;DR: This review not only summarizes the most common synthetic approaches for the generation of magnetic NPs, but also focuses on different surface modification strategies that are used today to enhance the biocompatibility of these NPs.
Book ChapterDOI
Lysozyme: a model protein for amyloid research.
Rajaram Swaminathan,Vijay Kumar Ravi,Satish Kumar,Mattaparthi Venkata Satish Kumar,Nividh Chandra +4 more
TL;DR: The rich information available on ly sozyme coupled with the multiple conditions that have been successful in inducing/inhibiting its aggregation in vitro makes lysozyme an ideal model protein to investigate amyloidogenesis.
References
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Sara Linse,Celia Cabaleiro-Lago,Wei-Feng Xue,Iseult Lynch,Stina Lindman,Eva Thulin,Sheena E. Radford,Kenneth A. Dawson +7 more
TL;DR: It is shown that nanoparticles (copolymer particles, cerium oxide particles, quantum dots, and carbon nanotubes) enhance the probability of appearance of a critical nucleus for nucleation of protein fibrils from human β2-microglobulin, and the shortened lag phase suggest a mechanism involving surface-assisted nucleation that may increase the risk for toxic cluster and amyloid formation.
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Phospholipid Catalysis of Diabetic Amyloid Assembly
TL;DR: In this paper, the authors use kinetic studies in conjunction with assessments of lipid binding and electron microscopy to investigate the interactions of IAPP with phospholipid bilayers and the morphological effects of membranes on IAPP fibers.
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Inducible Expression of Tau Repeat Domain in Cell Models of Tauopathy AGGREGATION IS TOXIC TO CELLS BUT CAN BE REVERSED BY INHIBITOR DRUGS
Inna Khlistunova,Jacek Biernat,Yipeng Wang,Marcus Pickhardt,Martin von Bergen,Zuzana Gazova,Eckhard Mandelkow,Eva-Maria Mandelkow +7 more
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