Metal-dependent inhibition of amyloid fibril formation: synergistic effects of cobalt–tannic acid networks

Zhang, Wenjie; Christofferson, Andrew J.; Besford, Quinn A.; Richardson, Joseph J.; Guo, Junling; Ju, Yi; Kempe, Kristian; Yarovsky, Irene; Caruso, Frank

doi:10.1039/c8nr09221d

Cited by 42 publications

(32 citation statements)

References 54 publications

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“…48 Self-destructive PEGylated nanosweepers composed of cationic CS captured Aβ and promoted their degradation through cell-mediated autophagy. 49 Metal-phenolic networks-coated AuNPs inhibited Aβ fibrillation, 50 sulfur NPs, 51 and polymerized o-phenylenediamine-derived carbon dots 52 decreased Cu 2+ -mediated Aβ aggregation, while iminodiacetic acid-conjugated, 53 d-penicillamine-capped selenium, 54 and PEG-modified-CS-NPs loaded with a Zn(II)-binding peptide 55 decreased Zn 2+ -mediated Aβ aggregation. MoO 3−x nanodots acted on the same target through the mimic of catalase and SOD activities, 56 and upconversion NPs disrupted amyloid plaques after NIR irradiation.…”

Section: Nanotechnologies Exploiting New Tools To Force Bbb Openingmentioning

confidence: 99%

<p>Innovative Therapies and Nanomedicine Applications for the Treatment of Alzheimer’s Disease: A State-of-the-Art (2017–2020)</p>

Binda¹,

Murano²,

Rivolta³

2020

IJN

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The field of nanomedicine is constantly expanding. Since the first work dated in 1999, almost 28 thousand articles have been published, and more and more are published every year: just think that only in the last five years 20,855 have come out (source PUBMED) including original research and reviews. The goal of this review is to present the current knowledge about nanomedicine in Alzheimer's disease, a widespread neurodegenerative disorder in the over 60 population that deeply affects memory and cognition. Thus, after a brief introduction on the pathology and on the state-of-the-art research for NPs passing the BBB, special attention is placed to new targets that can enter the interest of nanoparticle designers and to new promising therapies. The authors performed a literature review limited to the last three years (2017-2020) of available studies with the intention to present only novel formulations or approaches where at least in vitro studies have been performed. This choice was made because, while limiting the sector to nanotechnology applied to Alzheimer, an organic census of all the relevant news is difficult to obtain.

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Section: Nanotechnologies Exploiting New Tools To Force Bbb Openingmentioning

confidence: 99%

<p>Innovative Therapies and Nanomedicine Applications for the Treatment of Alzheimer’s Disease: A State-of-the-Art (2017–2020)</p>

Binda¹,

Murano²,

Rivolta³

2020

IJN

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“…Earlier studies reported contradictory effects of NPs on amyloid fibril formation ranging from a complete inhibition to strong acceleration of the process (Figure 1). 5,17–20 These paradoxical effects result from the diversity of NPs which are characterized by varying physicochemical properties, determined by their material, 9 surface chemistry, 21–23 morphology and size. 24–30 NP size effects on amyloid peptide aggregation have been the subject of intense research.…”

Section: Introductionmentioning

confidence: 99%

Size Matters: A Mechanistic Model of Nanoparticle Curvature Effects on Amyloid Fibril Formation

John

Adler

Elsner

et al. 2021

Preprint

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The aggregation of peptides into amyloid fibrils is linked to ageing-related diseases, such as Alzheimer's disease and type 2 diabetes. Interfaces, particularly those with large nanostructured surface areas, can affect the kinetics of peptide aggregation, ranging from a complete inhibition to strong acceleration. While a number of physiochemical parameters determine interface effects, we here focus on the role of nanoparticle curvature for the aggregation of the amyloidogenic peptides Aβ40, NNFGAIL, GNNQQNY and VQIYVK. Nanoparticles (NPs) provided a surface for peptide monomers to adsorb, enabling the nucleation into oligomers and fibril formation. High surface curvature, however, destabilized prefibrillar structures, providing an explanation for inhibitory effects on fibril growth. Thioflavin T (ThT) fluorescence assays as well as dynamic light scattering (DLS), atomic force microscopy (AFM) and electron microscopy experiments revealed NP size-dependent effects on amyloid fibril formation, with differences between the peptides. While 5 nm gold NPs (AuNP-5) retarded or inhibited the aggregation of most peptides, larger 20 nm gold NPs (AuNP-20) tended to accelerate peptide aggregation. Molecular dynamics (MD) studies demonstrated that NPs' ability to catalyze or inhibit oligomer formation was influenced by the oligomer stability at curved interfaces which was lower at more highly curved surfaces. Differences in the NP effects for the peptides resulted from the peptide properties (size, aggregation propensity) and concomitant surface binding affinities. The results can be applied to the design of future nanostructured materials for defined applications.

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“…[21] More recently, we used a combination of electronic structure calculations and classical MD simulations to elucidate the mechanisms by which metal-phenolic networks are able to inhibit fibril formation by the Alzheimer's disease implicated amyloid-b protein, which enabled us to shed light on this recently discovered phenomenon. [22] It must be noted, however, that despite the consistent growth of modelling applications and some evident success in employing simulations to understand the elusive process of amyloid fibril formation, there are still methodological challenges that must be carefully considered. Specifically, in-silico emulated biomolecular behaviour is governed by the accuracy of the underlying potential energy function, or forcefield, which describes all inter-atomic interactions in classical molecular mechanics simulations.…”

Section: Introductionmentioning

confidence: 99%

The Enigma of Amyloid Forming Proteins: Insights From Molecular Simulations

Todorova

Yarovsky

2019

Aust. J. Chem.

Self Cite

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Molecular level insight into the interplay between protein sequence, structure, and conformational dynamics is crucial for the comprehensive understanding of protein folding, misfolding, and aggregation phenomena that are pertinent to the formation of amyloid fibrils implicated in several degenerative diseases. Computational modelling provides insight into protein behaviour at spatial and temporal resolution still largely outside the reach of experiments. Herein we present an account of our theoretical modelling research conducted in collaboration with several experimental groups where we explored the effects of local environment on the structure and aggregation propensity of several types of amyloidogenic peptides and proteins, including apolipoprotein C-II, insulin, amylin, and amyloid-b using a variety of computational approaches.

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Metal-dependent inhibition of amyloid fibril formation: synergistic effects of cobalt–tannic acid networks

Abstract: Cobalt–tannic acid-coated gold nanoparticles are found to better inhibit amyloid fibril formation than other metal-based tannic acid-coated particles.

Cited by 42 publications

References 54 publications

<p>Innovative Therapies and Nanomedicine Applications for the Treatment of Alzheimer’s Disease: A State-of-the-Art (2017–2020)</p>

<p>Innovative Therapies and Nanomedicine Applications for the Treatment of Alzheimer’s Disease: A State-of-the-Art (2017–2020)</p>

Size Matters: A Mechanistic Model of Nanoparticle Curvature Effects on Amyloid Fibril Formation

The Enigma of Amyloid Forming Proteins: Insights From Molecular Simulations

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