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Amyloids

Amyloids is a collective term to describe misfolded proteins that self-assemble into insoluble fibrils both in vitro and in vivo. These protein aggregates are involved in a wide variety of human diseases, from Alzheimer's Disease to Type 2 Diabetes and Rheumatoid Arthritis to Artherosclerosis. Given the importance of amyloids in a disease context, intense study of their biophysical properties has given plenty of new information on ways to inhibit their formation.

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Characterizing Structural Stability of Amyloid Motif Fibrils Mediated by Water Molecules

Characterizing Structural Stability of Amyloid Motif Fibrils Mediated by Water Molecules

Water everywhere: The effect of interior water molecules on the properties and stabilities of amyloid fibrils is determined by molecular dynamics simulations.

[Article]
Hyunsung Choi, Hyun Joon Chang, Myeongsang Lee, Sungsoo Na
ChemPhysChem, February 22, 2017, https://doi.org/10.1002/cphc.201601327 Read article

Hematite-Based Photoelectrode Materials for Photoelectrocatalytic Inhibition of Alzheimer's β-Amyloid Self-Assembly

Hematite‐Based Photoelectrode Materials for Photoelectrocatalytic Inhibition of Alzheimer's β‐Amyloid Self‐Assembly

Hematite-based photoelectrode platform effectively inhibits β-amyloid (Aβ) aggregation through photoelectrocatalytic process. Upon illumination under anodic bias, the hematite photoanode generates hole-derived radicals (e.g., hydroxyl radicals, OH·) that trigger the oxidation of Aβ residues, blocking further aggregation. The cobalt phosphate co-catalyst deposited on the hematite photoanode enhances the inhibitory effect of the photoanode on Aβ aggregation.

[Communication]
Kayoung Kim, Byung Il Lee, You Jung Chung, Woo Seok Choi, Chan Beum Park
Adv. Healthcare Mater., February 14, 2017, https://doi.org/10.1002/adhm.201601133 Read article

Flexible N-Termini of Amyloid β-Protein Oligomers: A Link between Structure and Activity?

Flexible N‐Termini of Amyloid β‐Protein Oligomers: A Link between Structure and Activity?

[Review]
Brigita Urbanc
Isr. J. Chem., February 03, 2017, https://doi.org/10.1002/ijch.201600097 Read article

Theory of Amyloid Fibril Nucleation from Folded Proteins

Theory of Amyloid Fibril Nucleation from Folded Proteins

[Full Paper]
Lingyun Zhang, Jeremy D. Schmit
Isr. J. Chem., January 30, 2017, https://doi.org/10.1002/ijch.201600079 Read article

Investigation of the Subcellular Neurotoxicity of Amyloid-β Using a Device Integrating Microfluidic Perfusion and Chemotactic Guidance

Investigation of the Subcellular Neurotoxicity of Amyloid‐β Using a Device Integrating Microfluidic Perfusion and Chemotactic Guidance

By a combination of physical restriction and chemotactic guidance in a multicompartment microfluidic device, localized chemical treatment is performed to isolated axons or dendrites and the subcellular toxicity of amyloid-β peptides is investigated. This study demonstrates a localized intake or secretion of amyloid-β at axonal terminals, instead of dendrites that cause neuronal degeneration.

[Full Paper]
Wei Li, Zhen Xu, Bingzhe Xu, Chung Yuen Chan, Xudong Lin, Ying Wang, Ganchao Chen, Zhigang Wang, Qiuju Yuan, Guangyu Zhu, Hongyan Sun, Wutian Wu, Peng Shi
Adv. Healthcare Mater., January 25, 2017, https://doi.org/10.1002/adhm.201600895 Read article

Conformational Transitions of the Amyloid-β Peptide Upon Copper(II) Binding and pH Changes

Conformational Transitions of the Amyloid‐β Peptide Upon Copper(II) Binding and pH Changes

[Full Paper]
Qinghua Liao, Michael C. Owen, Olujide O. Olubiyi, Bogdan Barz, Birgit Strodel
Isr. J. Chem., January 20, 2017, https://doi.org/10.1002/ijch.201600108 Read article

Cerebrospinal Fluid Proteins as Regulators of Beta-amyloid Aggregation and Toxicity

Cerebrospinal Fluid Proteins as Regulators of Beta‐amyloid Aggregation and Toxicity

[Review]
Kayla M. Pate, Regina M. Murphy
Isr. J. Chem., January 18, 2017, https://doi.org/10.1002/ijch.201600078 Read article

The Amyloid-β Peptide in Amyloid Formation Processes: Interactions with Blood Proteins and Naturally Occurring Metal Ions

The Amyloid‐β Peptide in Amyloid Formation Processes: Interactions with Blood Proteins and Naturally Occurring Metal Ions

[Review]
Cecilia Wallin, Jinghui Luo, Jüri Jarvet, Sebastian K. T. S. Wärmländer, Astrid Gräslund
Isr. J. Chem., December 28, 2016, https://doi.org/10.1002/ijch.201600105 Read article

Evolutionary Adaptation and Amyloid Formation: Does the Reduced Amyloidogenicity and Cytotoxicity of Ursine Amylin Contribute to the Metabolic Adaption of Bears and Polar Bears?

Evolutionary Adaptation and Amyloid Formation: Does the Reduced Amyloidogenicity and Cytotoxicity of Ursine Amylin Contribute to the Metabolic Adaption of Bears and Polar Bears?

[Full Paper]
Rehana Akter, Andisheh Abedini, Zachary Ridgway, Xiaoxue Zhang, Joel Kleinberg, Ann Marie Schmidt, Daniel P. Raleigh
Isr. J. Chem., December 19, 2016, https://doi.org/10.1002/ijch.201600081 Read article

Fluorescent Markers for Amyloid-β Detection: Computational Insights

Fluorescent Markers for Amyloid‐β Detection: Computational Insights

[Review]
Francesca Peccati, Stefano Pantaleone, Xavier Solans-Monfort, Mariona Sodupe
Isr. J. Chem., December 01, 2016, https://doi.org/10.1002/ijch.201600114 Read article

Generation of Amyloid-β Peptides by γ-Secretase

Generation of Amyloid‐β Peptides by γ‐Secretase

[Review]
Rodrigo Aguayo-Ortiz, Laura Dominguez
Isr. J. Chem., November 25, 2016, https://doi.org/10.1002/ijch.201600073 Read article

Formation of Apoptosis-Inducing Amyloid Fibrils by Tryptophan

Formation of Apoptosis‐Inducing Amyloid Fibrils by Tryptophan

[Full Paper]
Shira Shaham-Niv, Pavel Rehak, Lela Vuković, Lihi Adler-Abramovich, Petr Král, Ehud Gazit
Isr. J. Chem., November 16, 2016, https://doi.org/10.1002/ijch.201600076 Read article

Molecular Simulations of Amyloid Structures, Toxicity, and Inhibition

Molecular Simulations of Amyloid Structures, Toxicity, and Inhibition

[Review]
Mingzhen Zhang, Baiping Ren, Hong Chen, Yan Sun, Jie Ma, Binbo Jiang, Jie Zheng
Isr. J. Chem., November 16, 2016, https://doi.org/10.1002/ijch.201600075 Read article

Structural Biology of Calcitonin: From Aqueous Therapeutic Properties to Amyloid Aggregation

Structural Biology of Calcitonin: From Aqueous Therapeutic Properties to Amyloid Aggregation

[Review]
Kian Kamgar-Parsi, James Tolchard, Birgit Habenstein, Antoine Loquet, Akira Naito, Ayyalusamy Ramamoorthy
Isr. J. Chem., November 15, 2016, https://doi.org/10.1002/ijch.201600096 Read article

Compilation and Analysis of Enzymes, Engineered Antibodies, and Nanoparticles Designed to Interfere with Amyloid-β Aggregation

Compilation and Analysis of Enzymes, Engineered Antibodies, and Nanoparticles Designed to Interfere with Amyloid‐β Aggregation

[Review]
Jun Zhao, Buyong Ma, Ruth Nussinov
Isr. J. Chem., October 25, 2016, https://doi.org/10.1002/ijch.201600093 Read article

Coarse-grained and All-atom Simulations towards the Early and Late Steps of Amyloid Fibril Formation

Coarse‐grained and All‐atom Simulations towards the Early and Late Steps of Amyloid Fibril Formation

[Review]
Mara Chiricotto, Thanh Thuy Tran, Phuong H. Nguyen, Simone Melchionna, Fabio Sterpone, Philippe Derreumaux
Isr. J. Chem., August 01, 2016, https://doi.org/10.1002/ijch.201600048 Read article

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