Literature DB >> 29886534

Kinetic Analysis of Amyloid Formation.

Georg Meisl1, Thomas C T Michaels2,3, Sara Linse4, Tuomas P J Knowles2,5.   

Abstract

The formation of amyloid fibrils is a central phenomenon in the progressive pathology of many neurodegenerative diseases, as well as in the fabrication of functional materials. Several different molecular processes acting in concert are responsible for the formation of amyloid fibrils from monomeric protein in solution. Here, we describe a method to determine which microscopic processes drive the overall formation of fibrils by using chemical kinetics in combination with systematic experimental datasets analysed in a global manner. We outline general concepts for obtaining suitable kinetic data and detail the key stages of data analysis, from quality control to the verification of a specific mechanism of aggregation.

Entities:  

Keywords:  Amyloid fibrils; Kinetic modeling; Molecular-level mechanism; Protein aggregation; Self-assembly

Mesh：

Substances：

Year:  2018        PMID： 29886534     DOI： 10.1007/978-1-4939-7816-8_12

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN： 1064-3745


  7 in total

1.  Dynamics of Amyloid Formation from Simplified Representation to Atomistic Simulations.

Authors:  Phuong Hoang Nguyen; Pierre Tufféry; Philippe Derreumaux
Journal:  Methods Mol Biol       Date:  2022

Review 2.  Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer's Disease, Parkinson's Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis.

Authors:  Phuong H Nguyen; Ayyalusamy Ramamoorthy; Bikash R Sahoo; Jie Zheng; Peter Faller; John E Straub; Laura Dominguez; Joan-Emma Shea; Nikolay V Dokholyan; Alfonso De Simone; Buyong Ma; Ruth Nussinov; Saeed Najafi; Son Tung Ngo; Antoine Loquet; Mara Chiricotto; Pritam Ganguly; James McCarty; Mai Suan Li; Carol Hall; Yiming Wang; Yifat Miller; Simone Melchionna; Birgit Habenstein; Stepan Timr; Jiaxing Chen; Brianna Hnath; Birgit Strodel; Rakez Kayed; Sylvain Lesné; Guanghong Wei; Fabio Sterpone; Andrew J Doig; Philippe Derreumaux
Journal:  Chem Rev       Date:  2021-02-05       Impact factor: 60.622

3.  Amyloid-β peptide 37, 38 and 40 individually and cooperatively inhibit amyloid-β 42 aggregation.

Authors:  Gabriel A Braun; Alexander J Dear; Kalyani Sanagavarapu; Henrik Zetterberg; Sara Linse
Journal:  Chem Sci       Date:  2022-02-07       Impact factor: 9.825

4.  Amyloid Fibril Formation of Arctic Amyloid-β 1-42 Peptide is Efficiently Inhibited by the BRICHOS Domain.

Authors:  Xueying Zhong; Rakesh Kumar; Yu Wang; Henrik Biverstål; Caroline Ingeborg Jegerschöld; Philip J B Koeck; Jan Johansson; Axel Abelein; Gefei Chen
Journal:  ACS Chem Biol       Date:  2022-07-25       Impact factor: 4.634

5.  Toward high-throughput oligomer detection and classification for early-stage aggregation of amyloidogenic protein.

Authors:  Bogachan Tahirbegi; Alastair J Magness; Maria Elena Piersimoni; Xiangyu Teng; James Hooper; Yuan Guo; Thomas Knöpfel; Keith R Willison; David R Klug; Liming Ying
Journal:  Front Chem       Date:  2022-08-30       Impact factor: 5.545

6.  Key Residues for the Formation of Aβ42 Amyloid Fibrils.

Authors:  Frederick Hsu; Giovanna Park; Zhefeng Guo
Journal:  ACS Omega       Date:  2018-07-31

7.  Augmentation of Bri2 molecular chaperone activity against amyloid-β reduces neurotoxicity in mouse hippocampus in vitro.

Authors:  Gefei Chen; Yuniesky Andrade-Talavera; Simone Tambaro; Axel Leppert; Harriet E Nilsson; Xueying Zhong; Michael Landreh; Per Nilsson; Hans Hebert; Henrik Biverstål; André Fisahn; Axel Abelein; Jan Johansson
Journal:  Commun Biol       Date:  2020-01-20
  7 in total

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