Article
Chemistry, Multidisciplinary
Ewelina Stefaniak, Elena Atrian-Blasco, Wojciech Goch, Laurent Sabater, Christelle Hureau, Wojciech Bal
Summary: This study investigated the effect of Cu-II on the aggregation of A beta(1-40) and A beta(4-40). It was found that substoichiometric Cu-II concentrations accelerated aggregation, while superstoichiometric Cu-II inhibited fibril formation. The interaction between Cu-II, A beta(4-40), and A beta(1-40) resulted in significant changes in the aggregation process.
CHEMISTRY-A EUROPEAN JOURNAL
(2021)
Article
Chemistry, Physical
Baole Zhang, Taofeng Zhu, Lei Liu, Liang Yuan
Summary: This study developed an electrochemical detection method for monitoring the degradation of amyloid p oligomers. By directly electrooxidizing specific tyrosine residues within the oligomers, the degradation level could be measured, confirming the influence of Ap peptide structure on signal output. The method also displayed better sensitivity compared to dynamic light scattering, atomic force microscopy, and fluorescence assays.
JOURNAL OF COLLOID AND INTERFACE SCIENCE
(2023)
Review
Chemistry, Physical
Silvana Andreescu, Alina Vasilescu
Summary: Electrochemistry provides various methods for investigating protein aggregation and identifying biomarkers of neurodegenerative diseases, with biosensors playing a crucial role in this area. Recent research focuses on enhancing sensitivity, establishing correlations between protein structure and aggregation propensity, and exploring novel approaches to study protein aggregates in solution. Growing applications aim to accurately evaluate aggregate populations and go beyond proof of principle in method adoption.
CURRENT OPINION IN ELECTROCHEMISTRY
(2021)
Article
Chemistry, Physical
Jiuhong Zhao, Na Xu, Xiaotong Yang, Guixia Ling, Peng Zhang
Summary: Alzheimer's disease is the most common form of dementia in humans, and it is related to the misfolding and aggregation of Aβ peptides. Gold nanoparticles have excellent properties and can be used in the diagnosis and drug delivery for AD.
COLLOID AND INTERFACE SCIENCE COMMUNICATIONS
(2022)
Article
Biotechnology & Applied Microbiology
Bing-Yu Wang, Bien-Chen Gu, Gou-Jen Wang, Yuan-Han Yang, Chia-Che Wu
Summary: This study demonstrates that a nanostructured gold electrode with deposited gold nanoparticles induced via electrochemical impedance spectroscopy (EIS) can be used as a conformation biosensor for the detection of Amyloid-beta(1-42) (A beta(1-42)) oligomers associated with Alzheimer's disease. The concentration of different A beta(1-42) conformations can be determined using EIS analysis with an equivalent circuit model. Probe antibodies (12F4) are used to identify the conformations of A beta(1-42) monomers and oligomers.
FRONTIERS IN BIOENGINEERING AND BIOTECHNOLOGY
(2022)
Article
Biochemistry & Molecular Biology
Yin-Lei Han, Huan-Huan Yin, Chao Xiao, Matthew T. Bernards, Yi He, Yi-Xin Guan
Summary: This study investigates the inhibitory effects of four polyphenols (brazilin, resveratrol, hematoxylin, and rosmarinic acid) on the aggregation of amyloid beta (A beta) proteins associated with Alzheimer's disease (AD). Molecular dynamics simulations reveal the different binding sites and destabilizing mechanisms of the polyphenols on the A beta 17-42 pentamer. The findings provide insights into the interactions between the polyphenols and A beta aggregation, which can guide the screening and design of effective AD drugs.
ACS CHEMICAL NEUROSCIENCE
(2023)
Review
Medicine, Research & Experimental
Yan Zheng, Limin Zhang, Jinge Zhao, Lingyun Li, Minxuan Wang, Peifeng Gao, Qing Wang, Xiaoling Zhang, Weizhi Wang
Summary: Alzheimer's disease is an irreversible neurodegenerative disease with challenges in early diagnosis and treatment. The 3-β amyloid protein is an important biomarker, and aptamers play a crucial role in AD theranostics.
Article
Chemistry, Multidisciplinary
Anil Koklu, Shofarul Wustoni, Valentina-Elena Musteata, David Ohayon, Maximilian Moser, Iain McCulloch, Suzana P. Nunes, Sahika Inal
Summary: Alzheimer's disease is a neurodegenerative disorder with no specific cure, emphasizing the importance of early diagnosis. A common pathological change in AD-affected brains is the accumulation of Aβ protein into plaques, which was detected using a micron-scale OECT in this study.
Article
Food Science & Technology
Bong-Geum Jang, Jisun Lee, Boyoung Choi, Young Ho Koh, Min-Ju Kim
Summary: Resveratrol, a drug candidate for Alzheimer's disease, has shown beneficial effects in various models but may paradoxically increase Aβ production. This effect may be mediated by AMPK-proteasome signaling pathway.
FOOD AND CHEMICAL TOXICOLOGY
(2021)
Review
Biochemistry & Molecular Biology
Anna Sulatskaya, Anastasiia O. Kosolapova, Alexander G. Bobylev, Mikhail Belousov, Kirill S. Antonets, Maksim Sulatsky, Irina M. Kuznetsova, Konstantin K. Turoverov, Olesya Stepanenko, Anton A. Nizhnikov
Summary: Both amyloids and beta-barrel proteins have beta-sheet-rich structures, with the latter being able to form functional amyloids in vivo. These beta-barrel amyloid proteins can interact with each other and form toxic oligomers, potentially contributing to the development of amyloidoses. Rapidly growing discoveries suggest that the number and diversity of functions of amyloid-forming beta-barrel proteins are significantly greater than currently understood.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2021)
Article
Biochemistry & Molecular Biology
Jufei Xu, Ting Zheng, Xiangyi Huang, Yanan Wang, Guowei Yin, Weihong Du
Summary: This study investigated the inhibition of procyanidine on hIAPP and A beta aggregation through diverse biophysical and biochemical methods. Procyanidine effectively inhibited the aggregation of both peptides through hydrophobic and hydrogen bonding interactions, dissolved aged fibrils into nanoscale particles, and ameliorated cytotoxicity and membrane leakage. The compound showed better binding affinity and inhibitory effects on hIAPP, suggesting its potential as a prospective inhibitor against hIAPP, offering a possible strategy for T2DM and AD treatments.
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2021)
Article
Biochemistry & Molecular Biology
Edward Chau, Hyunjoo Kim, Jineun Shin, Alberto Martinez, Jin Ryoun Kim
Summary: The study found that AM17 can not only inhibit the aggregation of alpha S monomers, but also disaggregate alpha S oligomers and fibrils, independent of copper ions. Resveratrol also showed similar inhibitory effects on alpha S aggregation only in the presence of copper ions.
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
(2021)
Article
Chemistry, Analytical
Qisheng Luo, Dehong Yu, Zichun Song, Jiuying Cui, Yuanxun Gong, Qianli Tang, Xianjiu Liao, Ning Xin, Fenglei Gao
Summary: We have developed a bipedal driven catalytic hairpin assembly for the electrochemical detection of highly sensitive amyloid-beta oligomers. Aptamers specifically recognize of amyloid-beta oligomers can activate catalytic hairpin assembly and form bipedal molecular machines, achieving amplification of the electrochemical signal. This enzyme-free detection method can realize high sensitivity and specificity detection of multiple target proteins, and has reference significance and application value in the field of biological detection.
SENSORS AND ACTUATORS B-CHEMICAL
(2023)
Article
Engineering, Biomedical
Bibin Anand, Qi Wu, Maryam Nakhaei-Nejad, Govindarajan Karthivashan, Lyudmyla Dorosh, Sara Amidian, Abhishek Dahal, Xiuju Li, Maria Stepanova, Holger Wille, Fabrizio Giuliani, Satyabrata Kar
Summary: Native PLGA nanoparticles show therapeutic potential in the treatment of Alzheimer's disease by suppressing aggregation of beta-amyloid peptides, triggering their disassembly, reducing phosphorylation of tau protein, enhancing neuronal viability, and attenuating memory deficits and A beta levels in animal models of AD.
BIOACTIVE MATERIALS
(2022)
Article
Biochemistry & Molecular Biology
Panagiotis M. Spatharas, Georgia I. Nasi, Paraskevi L. Tsiolaki, Marilena K. Theodoropoulou, Nikos C. Papandreou, Andreas Hoenger, Ioannis P. Trougakos, Vassiliki A. Iconomidou
Summary: Clusterin is identified as a glycoprotein involved in amyloid formation and has aggregation-prone regions that can form amyloid-like fibrils while also inhibiting amyloid-beta fibril formation. These findings suggest a potential role of clusterin in the molecular mechanism of inhibiting amyloid formation and indicate a possible involvement of molecular chaperones with amyloidogenic properties in regulating amyloid formation.
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE
(2022)
