Porous Materials for Early Diagnosis of Neurodegenerative Diseases DOI Creative Commons
Payam Arghavani, Hossein Daneshgar, Soheil Sojdeh

et al.

Advanced Healthcare Materials, Journal Year: 2025, Volume and Issue: unknown

Published: Jan. 6, 2025

Abstract Neurodegenerative diseases, particularly Alzheimer's disease and Parkinson's disease, present formidable challenges in modern medicine due to their complex pathologies the absence of curative treatments. Despite advances symptomatic management, early diagnosis remains essential for mitigating progression improving patient outcomes. Traditional diagnostic methods, such as MRI, PET, cerebrospinal fluid biomarker analysis, are often inadequate detection these diseases. Emerging porous materials, including metal–organic frameworks (MOFs), covalent–organic (COFs), MXene, zeolites, silicon, offer promising new approaches neurodegenerative These characterized by highly tunable physicochemical properties, have potential capture concentrate disease‐specific biomarkers amyloid‐beta (Aβ), tau protein, alpha‐synuclein (α‐Syn). The integration materials into advanced biosensors real‐time holds promise revolutionizing neurodiagnostic, enabling non‐invasive, sensitive, specific platforms. Furthermore, incorporation artificial intelligence (AI) machine learning (ML) techniques analysis sensor data enhances accuracy allows more efficient interpretation profiles. AI ML can optimize feature selection, improve pattern recognition, facilitate prediction progression, making them indispensable tools personalized medicine. This review explores diagnostics, emphasizing design, functionality, synergistic role advancing clinical applications.

Language: Английский

Supramolecular polymerization through kinetic pathway control and living chain growth DOI

Marius Wehner,

Frank Würthner

Nature Reviews Chemistry, Journal Year: 2019, Volume and Issue: 4(1), P. 38 - 53

Published: Dec. 21, 2019

Language: Английский

Citations

492
Half a century of amyloids: past, present and future DOI Creative Commons
Pu Chun Ke, Ruhong Zhou, Louise C. Serpell

et al.

Chemical Society Reviews, Journal Year: 2020, Volume and Issue: 49(15), P. 5473 - 5509

Published: Jan. 1, 2020

Amyloid diseases are global epidemics with profound health, social and economic implications yet remain without a cure. This dire situation calls for research into the origin pathological manifestations of amyloidosis to stimulate continued development new therapeutics. In basic science engineering, cross-β architecture has been constant thread underlying structural characteristics functional amyloids, realizing that amyloid structures can be both in nature fuelled innovations artificial whose use today ranges from water purification 3D printing. At conclusion half century since Eanes Glenner's seminal study amyloids humans, this review commemorates occasion by documenting major milestones date, perspectives biology, biophysics, medicine, microbiology, engineering nanotechnology. We also discuss challenges opportunities drive interdisciplinary field moving forward.

Language: Английский

Citations

486
Food protein amyloid fibrils: Origin, structure, formation, characterization, applications and health implications DOI
Yiping Cao, Raffaele Mezzenga

Advances in Colloid and Interface Science, Journal Year: 2019, Volume and Issue: 269, P. 334 - 356

Published: May 10, 2019

Language: Английский

Citations

465
Supramolecular Polymorphism in One-Dimensional Self-Assembly by Kinetic Pathway Control DOI

Marius Wehner,

Merle I. S. Röhr, Michael Bühler

et al.

Journal of the American Chemical Society, Journal Year: 2019, Volume and Issue: 141(14), P. 6092 - 6107

Published: March 20, 2019

Controlling polymorphism in molecular solids is of great interest since the properties and performances materials depend on molecules' mutual packing arrangements. Herein, we describe a perylene bisimide (PBI) organogelator molecule PBI-4 that self-assembles into three different one-dimensional supramolecular polymorphs (Agg 1-3) same solvent at concentration room temperature. The were characterized by UV/vis, CD, fluorescence IR spectroscopy, atomic force microscopy (AFM), theoretical calculations, revealing their arrangements are governed distinct π-π-stacking modes unique hydrogen-bonding patterns. Nudged elastic band (NEB) calculations for nucleation processes toward Agg 2 3 indicate starts from central kinetically trapped state 1 involves reorganization dimers. Time-, concentration-, temperature-dependent UV/vis experiments provided insights thermodynamic stability kinetics interconversion. On basis this information production certain polymorph could be accomplished either physically ultrasonication or chemically seeding. This work contributes to understanding lowest level hierarchy generation self-assembled 1D aggregate structures.

Language: Английский

Citations

256
The viral protein corona directs viral pathogenesis and amyloid aggregation DOI Creative Commons
Kariem Ezzat, Maria Pernemalm, Sandra Pålsson

et al.

Nature Communications, Journal Year: 2019, Volume and Issue: 10(1)

Published: May 27, 2019

Artificial nanoparticles accumulate a protein corona layer in biological fluids, which significantly influences their bioactivity. As nanosized obligate intracellular parasites, viruses share many biophysical properties with artificial extracellular environments and here we show that respiratory syncytial virus (RSV) herpes simplex type 1 (HSV-1) rich distinctive different fluids. Moreover, pre-coating differentially affects viral infectivity immune cell activation. In addition, demonstrate bind amyloidogenic peptides catalyze amyloid formation via surface-assisted heterogeneous nucleation. Importantly, HSV-1 catalyzes the aggregation of β-peptide (Aβ

Language: Английский

Citations

191
Plant Protein Amyloid Fibrils for Multifunctional Sustainable Materials DOI Creative Commons
Ting Li, Jiangtao Zhou, Mohammad Peydayesh

et al.

Advanced Sustainable Systems, Journal Year: 2023, Volume and Issue: 7(4)

Published: Jan. 12, 2023

Abstract Artificial functional materials based on amyloid fibrils are proven to be a promising strategy toward materials. However, scaling‐up applications present sustainability concerns, as animal proteins the main sources for fabricating fibrils. Plant‐protein‐based fibrils, more sustainable alternative proteins, attracting increasing interests building blocks in Herein, 11 different from wide range of plants evaluated, and comprehensive analysis seven species plant including kidney bean, black cowpea, mung chickpea, lentil, pumpkin seed, with an excellent ability form is presented. A universal diversity protein extraction fibrillization applied. Flexible persistence length ≈100 nm rigid several micrometers discovered 7S/8S 11S subunits dominated protein, respectively. Structural evolution β‐sheet content these proteinaceous assemblies characterized by thioflavin T (ThT) intensity, circular dichroism (CD) spectra, attenuated total reflectance‐Fourier transform infrared (ATR‐FTIR) typical angle X‐ray scattering (WAXS) spectra. Finally, their multifunctional further explored that amyloids demonstrate performance renewable degradable bioplastics, water purification membranes heavy metal removal.

Language: Английский

Citations

67
Protein Misfolding and Aggregation in Proteinopathies: Causes, Mechanism and Cellular Response DOI Creative Commons

Mohammad Ajmal

Diseases, Journal Year: 2023, Volume and Issue: 11(1), P. 30 - 30

Published: Feb. 9, 2023

Proteins are central to life functions. Alterations in the structure of proteins reflected their function. Misfolded and aggregates present a significant risk cell. Cells have diverse but integrated network protection mechanisms. Streams misfolded that cells continuously exposed must be continually monitored by an elaborated molecular chaperones protein degradation factors control contain misfolding problems. Aggregation inhibition properties small molecules such as polyphenols important they possess other beneficial antioxidative, anti-inflammatory, pro-autophagic help neuroprotection. A candidate with desired features is for any possible treatment development aggregation diseases. There need study phenomenon so we can treat some worst kinds human ailments related aggregation.

Language: Английский

Citations

50
Remodeling mechanism of gel network structure of soy protein isolate amyloid fibrils mediated by cellulose nanocrystals DOI

Qianxin Zhou,

Sixu Lv,

Wenqi Wang

et al.

Carbohydrate Polymers, Journal Year: 2024, Volume and Issue: 332, P. 121919 - 121919

Published: Feb. 9, 2024

Language: Английский

Citations

39
Atomic force microscopy for single molecule characterisation of protein aggregation DOI Creative Commons
Francesco Simone Ruggeri, Tomas Šneideris, Michele Vendruscolo

et al.

Archives of Biochemistry and Biophysics, Journal Year: 2019, Volume and Issue: 664, P. 134 - 148

Published: Feb. 10, 2019

The development of atomic force microscopy (AFM) has opened up a wide range novel opportunities in nanoscience and new modalities observation complex biological systems. AFM imaging been widely employed to resolve the heterogeneous conformational states involved protein aggregation at single molecule scale shed light onto molecular basis variety human pathologies, including neurodegenerative disorders. study individual macromolecules nanoscale, however, remains challenging, especially when fully quantitative information is required. In this review, we first discuss principles with special emphasis on fundamental factors defining its sensitivity accuracy. We then review parameters approaches work limit resolution order perform statistical analysis biomolecules nanoscale aggregates. This approach proved be powerful unravel hierarchical assembly misfolded species present transiently during aggregation, visualise their dynamics as well structural properties amyloid-inspired functional nanomaterials.

Language: Английский

Citations

128
Mitigation of Amyloidosis with Nanomaterials DOI
Pu Chun Ke, Emily H. Pilkington, Yunxiang Sun

et al.

Advanced Materials, Journal Year: 2019, Volume and Issue: 32(18)

Published: June 11, 2019

Abstract Amyloidosis is a biophysical phenomenon of protein aggregation with biological and pathogenic implications. Among the various strategies developed to date, nanomaterials multifunctional nanocomposites possessing certain structural physicochemical traits are promising candidates for mitigating amyloidosis in vitro vivo. The mechanisms underpinning toxicity introduced, opportunities materials science drive this interdisciplinary field forward highlighted. Advancement emerging frontier hinges on exploitation self‐assembly interactions amyloid proteins nanoparticles, intracellular extracellular proteins, chaperones, membranes, organelles, biometals.

Language: Английский

Citations

119