Literature DB >> 18412209

Amyloids: not only pathological agents but also ordered nanomaterials.

Izhack Cherny1, Ehud Gazit.   

Abstract

Amyloid fibers constitute one of the most abundant and important naturally occurring self-associated assemblies. A variety of protein and peptide molecules with various amino acid sequences form these highly stable and well-organized assemblies under diverse conditions. These assemblies display phase states ranging from liquid crystals to rigid nanotubes. The potential applications of these supramolecular assemblies exceed those of synthetic polymers since the building blocks may introduce biological function in addition to mechanical properties. Here we review the structural characteristics of amyloidal supramolecular assemblies, their potential use as either natural or de novo designed sequences, and the range of applications that have been demonstrated so far.

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Year:  2008        PMID: 18412209     DOI: 10.1002/anie.200703133

Source DB:  PubMed          Journal:  Angew Chem Int Ed Engl        ISSN: 1433-7851            Impact factor:   15.336


  84 in total

1.  Effect of sequence variation on the mechanical response of amyloid fibrils probed by steered molecular dynamics simulation.

Authors:  Hlengisizwe Ndlovu; Alison E Ashcroft; Sheena E Radford; Sarah A Harris
Journal:  Biophys J       Date:  2012-02-07       Impact factor: 4.033

2.  Structural polymorphism in amyloids: new insights from studies with Y145Stop prion protein fibrils.

Authors:  Eric M Jones; Bo Wu; Krystyna Surewicz; Philippe S Nadaud; Jonathan J Helmus; Shugui Chen; Christopher P Jaroniec; Witold K Surewicz
Journal:  J Biol Chem       Date:  2011-10-15       Impact factor: 5.157

3.  Self-catalyzed growth of S layers via an amorphous-to-crystalline transition limited by folding kinetics.

Authors:  Sungwook Chung; Seong-Ho Shin; Carolyn R Bertozzi; James J De Yoreo
Journal:  Proc Natl Acad Sci U S A       Date:  2010-09-07       Impact factor: 11.205

4.  Effects of Congo red on aβ(1-40) fibril formation process and morphology.

Authors:  Partha Pratim Bose; Urmimala Chatterjee; Ling Xie; Jan Johansson; Emmanuelle Göthelid; Per I Arvidsson
Journal:  ACS Chem Neurosci       Date:  2010-02-03       Impact factor: 4.418

5.  A kinetic study of ovalbumin fibril formation: the importance of fragmentation and end-joining.

Authors:  Jason M D Kalapothakis; Ryan J Morris; Juraj Szavits-Nossan; Kym Eden; Sam Covill; Sean Tabor; Jay Gillam; Perdita E Barran; Rosalind J Allen; Cait E MacPhee
Journal:  Biophys J       Date:  2015-05-05       Impact factor: 4.033

Review 6.  Molecular interactions of amyloid nanofibrils with biological aggregation modifiers: implications for cytotoxicity mechanisms and biomaterial design.

Authors:  Durga Dharmadana; Nicholas P Reynolds; Charlotte E Conn; Céline Valéry
Journal:  Interface Focus       Date:  2017-06-16       Impact factor: 3.906

7.  Non-equilibrium nature of two-dimensional isotropic and nematic coexistence in amyloid fibrils at liquid interfaces.

Authors:  Sophia Jordens; Lucio Isa; Ivan Usov; Raffaele Mezzenga
Journal:  Nat Commun       Date:  2013       Impact factor: 14.919

Review 8.  Materiomics: biological protein materials, from nano to macro.

Authors:  Steven Cranford; Markus J Buehler
Journal:  Nanotechnol Sci Appl       Date:  2010-11-12

9.  Induced beta-barrel formation of the Alzheimer's Abeta25-35 oligomers on carbon nanotube surfaces: implication for amyloid fibril inhibition.

Authors:  Zhaoming Fu; Yin Luo; Philippe Derreumaux; Guanghong Wei
Journal:  Biophys J       Date:  2009-09-16       Impact factor: 4.033

10.  Salts drive controllable multilayered upright assembly of amyloid-like peptides at mica/water interface.

Authors:  Bin Dai; Seung-gu Kang; Tien Huynh; Haozhi Lei; Matteo Castelli; Jun Hu; Yi Zhang; Ruhong Zhou
Journal:  Proc Natl Acad Sci U S A       Date:  2013-05-06       Impact factor: 11.205

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