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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Water everywhere: The effect of interior water molecules on the properties and stabilities of amyloid fibrils is determined by molecular dynamics simulations.
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 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.
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
Isr. J. Chem., February 03, 2017, https://doi.org/10.1002/ijch.201600097 Read article
Lingyun Zhang, Jeremy D. Schmit
Isr. J. Chem., January 30, 2017, https://doi.org/10.1002/ijch.201600079 Read article
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.
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
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
Kayla M. Pate, Regina M. Murphy
Isr. J. Chem., January 18, 2017, https://doi.org/10.1002/ijch.201600078 Read article
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
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
Francesca Peccati, Stefano Pantaleone, Xavier Solans-Monfort, Mariona Sodupe
Isr. J. Chem., December 01, 2016, https://doi.org/10.1002/ijch.201600114 Read article
Rodrigo Aguayo-Ortiz, Laura Dominguez
Isr. J. Chem., November 25, 2016, https://doi.org/10.1002/ijch.201600073 Read article
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
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
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
Jun Zhao, Buyong Ma, Ruth Nussinov
Isr. J. Chem., October 25, 2016, https://doi.org/10.1002/ijch.201600093 Read article
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