Literature DB >> 31325011

Structure and Function of Alzheimer's Amyloid βeta Proteins from Monomer to Fibrils: A Mini Review.

Nikhil Agrawal1, Adam A Skelton2,3.   

Abstract

Alzheimer's disease is the most common form of dementia, that affects millions of people worldwide. According to the widely accepted amyloid cascade hypothesis, misfolding and aggregation of Aβ peptides is the principal cause of Alzheimer's disease. In the present mini-review, we have discussed the different structures of Aβ protein from monomer to fibrils and their arrangement in different symmetries. We have highlighted the critical amino acid residue that plays a crucial role in the early stage misfolding of Aβ monomers, Aβ fibrils arrangement in different symmetries, the elongation process and Aβ protein interaction with the membrane. We have further discussed the antibodies that are currently in clinical trial phase III for Alzheimer's disease.

Entities:  

Keywords:  Alzheimer’s disease; Amyloid βeta peptide; Bapineuzumab; Solanezumab; Tramiprosate

Year:  2019        PMID: 31325011     DOI: 10.1007/s10930-019-09854-3

Source DB:  PubMed          Journal:  Protein J        ISSN: 1572-3887            Impact factor:   2.371


  105 in total

1.  Dynamics of amyloid β fibrils revealed by solid-state NMR.

Authors:  Holger A Scheidt; Isabel Morgado; Sven Rothemund; Daniel Huster
Journal:  J Biol Chem       Date:  2011-11-30       Impact factor: 5.157

2.  Structural characterization of a soluble amyloid beta-peptide oligomer.

Authors:  Liping Yu; Rohinton Edalji; John E Harlan; Thomas F Holzman; Ana Pereda Lopez; Boris Labkovsky; Heinz Hillen; Stefan Barghorn; Ulrich Ebert; Paul L Richardson; Laura Miesbauer; Larry Solomon; Diane Bartley; Karl Walter; Robert W Johnson; Philip J Hajduk; Edward T Olejniczak
Journal:  Biochemistry       Date:  2009-03-10       Impact factor: 3.162

3.  Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils.

Authors:  Michael T Colvin; Robert Silvers; Qing Zhe Ni; Thach V Can; Ivan Sergeyev; Melanie Rosay; Kevin J Donovan; Brian Michael; Joseph Wall; Sara Linse; Robert G Griffin
Journal:  J Am Chem Soc       Date:  2016-07-14       Impact factor: 15.419

4.  Alzheimer's abeta(1-40) amyloid fibrils feature size-dependent mechanical properties.

Authors:  Zhiping Xu; Raffaella Paparcone; Markus J Buehler
Journal:  Biophys J       Date:  2010-05-19       Impact factor: 4.033

5.  Imaging real-time aggregation of amyloid beta protein (1-42) by atomic force microscopy.

Authors:  Ashok Parbhu; Hai Lin; Julian Thimm; Ratneshwar Lal
Journal:  Peptides       Date:  2002-07       Impact factor: 3.750

6.  Aβ(1-42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease.

Authors:  Yiling Xiao; Buyong Ma; Dan McElheny; Sudhakar Parthasarathy; Fei Long; Minako Hoshi; Ruth Nussinov; Yoshitaka Ishii
Journal:  Nat Struct Mol Biol       Date:  2015-05-04       Impact factor: 15.369

7.  Crystal structure reveals conservation of amyloid-β conformation recognized by 3D6 following humanization to bapineuzumab.

Authors:  Hadar Feinberg; José W Saldanha; Linnea Diep; Amita Goel; Angela Widom; Geertruida M Veldman; William I Weis; Dale Schenk; Guriqbal S Basi
Journal:  Alzheimers Res Ther       Date:  2014-06-02       Impact factor: 6.982

8.  Amyloid-β oligomers are sequestered by both intracellular and extracellular chaperones.

Authors:  Priyanka Narayan; Sarah Meehan; John A Carver; Mark R Wilson; Christopher M Dobson; David Klenerman
Journal:  Biochemistry       Date:  2012-11-08       Impact factor: 3.162

9.  Lipids revert inert Abeta amyloid fibrils to neurotoxic protofibrils that affect learning in mice.

Authors:  Ivo Cristiano Martins; Inna Kuperstein; Hannah Wilkinson; Elke Maes; Mieke Vanbrabant; Wim Jonckheere; Patrick Van Gelder; Dieter Hartmann; Rudi D'Hooge; Bart De Strooper; Joost Schymkowitz; Frederic Rousseau
Journal:  EMBO J       Date:  2007-12-06       Impact factor: 11.598

10.  X-ray crystallographic structures of trimers and higher-order oligomeric assemblies of a peptide derived from Aβ(17-36).

Authors:  Ryan K Spencer; Hao Li; James S Nowick
Journal:  J Am Chem Soc       Date:  2014-04-03       Impact factor: 15.419

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  4 in total

Review 1.  Journey on Naphthoquinone and Anthraquinone Derivatives: New Insights in Alzheimer's Disease.

Authors:  Marta Campora; Valeria Francesconi; Silvia Schenone; Bruno Tasso; Michele Tonelli
Journal:  Pharmaceuticals (Basel)       Date:  2021-01-05

Review 2.  The Amyloid-β Pathway in Alzheimer's Disease.

Authors:  Harald Hampel; John Hardy; Kaj Blennow; Christopher Chen; George Perry; Seung Hyun Kim; Victor L Villemagne; Paul Aisen; Michele Vendruscolo; Takeshi Iwatsubo; Colin L Masters; Min Cho; Lars Lannfelt; Jeffrey L Cummings; Andrea Vergallo
Journal:  Mol Psychiatry       Date:  2021-08-30       Impact factor: 15.992

3.  Structural characterisation of amyloid-like fibrils formed by an amyloidogenic peptide segment of β-lactoglobulin.

Authors:  Vasantha Gowda; Michal Biler; Andrei Filippov; Malisa V Mantonico; Eirini Ornithopoulou; Mathieu Linares; Oleg N Antzutkin; Christofer Lendel
Journal:  RSC Adv       Date:  2021-08-17       Impact factor: 4.036

4.  Early stages of misfolding of PAP248-286 at two different pH values: An insight from molecular dynamics simulations.

Authors:  Nikhil Agrawal; Emilio Parisini
Journal:  Comput Struct Biotechnol J       Date:  2022-09-03       Impact factor: 6.155

  4 in total

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