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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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Direct Visualization of Model Membrane Remodeling by α-Synuclein Fibrillization

Direct Visualization of Model Membrane Remodeling by α‐Synuclein Fibrillization

Membrane remodeling by amyloid fibrils: Aggregation of the protein α-synuclein at the surface of negatively charged vesicle membrane results in the formation of membrane facets and lipid extraction.

[Article]
Himanshu Chaudhary, Vinod Subramaniam, Mireille M. A. E. Claessens
ChemPhysChem, April 27, 2017, https://doi.org/10.1002/cphc.201700050 Read article

Inhibitory Mechanism of Epigallocatechin Gallate on Fibrillation and Aggregation of Amidated Human Islet Amyloid Polypeptide

Inhibitory Mechanism of Epigallocatechin Gallate on Fibrillation and Aggregation of Amidated Human Islet Amyloid Polypeptide

What is the main interaction site? The inhibitory mechanism of epigallocatechin gallate (EGCG) on fibrillation of human islet amyloid polypeptide (hIAPP)-NH2 was illustrated by experimental and computational methods. The hydrogen bonding and π–π interactions between the A ring of EGCG and residue Phe23 (see graphic, A) as well as the hydrophobic interaction between the A ring of EGCG and residue Ile26 (see graphic, B) are the main driving force of this inhibition process.

[Article]
Zhi-Xue Xu, Gong-Li Ma, Qiang Zhang, Cong-Heng Chen, Yan-Ming He, Li-Hui Xu, Guang-Rong Zhou, Zhen-Hua Li, Hong-Jie Yang, Ping Zhou
ChemPhysChem, April 26, 2017, https://doi.org/10.1002/cphc.201700057 Read article

Benzylphenylpyrrolizinones with Anti-amyloid and Radical Scavenging Effects, Potentially Useful in Alzheimer's Disease Treatment

Benzylphenylpyrrolizinones with Anti‐amyloid and Radical Scavenging Effects, Potentially Useful in Alzheimer's Disease Treatment

Pick up & break up: This study aimed at increasing the radical scavenging and anti-Aβ-aggregation activities of a series of benzylidenephenylpyrrolizinones. Some of the new derivatives showed promising results in this regard. These compounds could serve as a good starting point for new drugs to treat Alzheimer's disease.

[Communication]
Jean-Pierre Jourdan, Marc Since, Laïla El Kihel, Cédric Lecoutey, Sophie Corvaisier, Rémi Legay, Jana Sopková-de Oliveira Santos, Thierry Cresteil, Aurélie Malzert-Fréon, Christophe Rochais, Patrick Dallemagne
ChemMedChem, April 12, 2017, https://doi.org/10.1002/cmdc.201700102 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

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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