Literature DB >> 14757044

Engineering amyloidogenicity towards the development of nanofibrillar materials.

Daizo Hamada1, Itaru Yanagihara, Kouhei Tsumoto.   

Abstract

When folded into their native structures, proteins in biological systems function as nanostructured machines. By contrast, some polypeptides tend to aggregate into other well-ordered structures, namely amyloid fibrils. Such well-ordered protein fibrils are attractive materials for nanobiotechnology because they self-associate through noncovalent bonds under controlled conditions - a property that is shared with small organic molecules called organogelators. Recently, the use of amyloid fibrils as structural templates for constructing nanowires has been demonstrated. Such applications will potentially become one of the next trends in protein engineering and nanobiotechnology.

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Year:  2004        PMID: 14757044     DOI: 10.1016/j.tibtech.2003.12.003

Source DB:  PubMed          Journal:  Trends Biotechnol        ISSN: 0167-7799            Impact factor:   19.536


  8 in total

Review 1.  Prevention of amyloid-like aggregation as a driving force of protein evolution.

Authors:  Elodie Monsellier; Fabrizio Chiti
Journal:  EMBO Rep       Date:  2007-08       Impact factor: 8.807

2.  The distribution of residues in a polypeptide sequence is a determinant of aggregation optimized by evolution.

Authors:  Elodie Monsellier; Matteo Ramazzotti; Patrizia Polverino de Laureto; Gian-Gaetano Tartaglia; Niccolò Taddei; Angelo Fontana; Michele Vendruscolo; Fabrizio Chiti
Journal:  Biophys J       Date:  2007-08-31       Impact factor: 4.033

3.  Oriented epitaxial growth of amyloid fibrils of the N27C mutant beta 25-35 peptide.

Authors:  Arpád Karsai; Unige Murvai; Katalin Soós; Botond Penke; Miklós S Z Kellermayer
Journal:  Eur Biophys J       Date:  2008-01-09       Impact factor: 1.733

4.  Modulation of self-association and subsequent fibril formation in an alanine-rich helical polypeptide.

Authors:  Ayben Top; Kristi L Kiick; Christopher J Roberts
Journal:  Biomacromolecules       Date:  2008-05-02       Impact factor: 6.988

5.  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

6.  Glycosaminoglycans promote fibril formation by amyloidogenic immunoglobulin light chains through a transient interaction.

Authors:  Douglas J Martin; Marina Ramirez-Alvarado
Journal:  Biophys Chem       Date:  2011-05-18       Impact factor: 2.352

7.  Structural and Mechanical Properties of Amyloid Beta Fibrils: A Combined Experimental and Theoretical Approach.

Authors:  Thomas J Paul; Zachary Hoffmann; Congzhou Wang; Maruda Shanmugasundaram; Jason DeJoannis; Alexander Shekhtman; Igor K Lednev; Vamsi K Yadavalli; Rajeev Prabhakar
Journal:  J Phys Chem Lett       Date:  2016-07-08       Impact factor: 6.475

8.  Lipid-modulated pharmacophore nanorods assembled at the air/water interface.

Authors:  Liron Philosof-Mazor; Roman Volinsky; Jurgen Jopp; Peter Blumberg; Hanna Rapaport; Victor E Marquez; Raz Jelinek
Journal:  Chemphyschem       Date:  2009-10-19       Impact factor: 3.102

  8 in total

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