Literature DB >> 21858783

Controlling the dimensions of amyloid fibrils: toward homogenous components for bionanotechnology.

Laura J Domigan1, Jackie P Healy, Susie J Meade, Richard J Blaikie, Juliet A Gerrard.   

Abstract

Amyloid fibrils have been recognized as having potential in a variety of bionanotechnological applications. However, realization of these applications is constrained by a lack of control over morphology and alignment, both crucial for potential end uses. This article focuses on the use of growth and storage conditions to control the length of amyloid fibrils formed from bovine insulin, with length distributions constructed from transmission electron microscopy (TEM) images. Growth temperature, pH, protein concentration, and storage conditions were examined and were seen to offer a range of conditions that favor different length distribution. The use of amyloid fibrils as nanowires is one area where control of fibril dimensions is desirable, for experimental setup and endpoint applications. The conductive properties of fibrils formed from bovine insulin are presented, with these insulin fibrils being shown to have high resistivity in their unmodified state, with current values in the nanoamp range. These low current values can be increased via modification, or the fibrils used in their native state in applications where low current values are desirable. These findings, coupled with the ability to predict and select for various insulin amyloid fibril dimensions, enhances their utility as nanomaterials.
Copyright © 2011 Wiley Periodicals, Inc.

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Year:  2011        PMID: 21858783     DOI: 10.1002/bip.21709

Source DB:  PubMed          Journal:  Biopolymers        ISSN: 0006-3525            Impact factor:   2.505


  5 in total

1.  Intrinsic electronic conductivity of individual atomically resolved amyloid crystals reveals micrometer-long hole hopping via tyrosines.

Authors:  Catharine Shipps; H Ray Kelly; Peter J Dahl; Sophia M Yi; Dennis Vu; David Boyer; Calina Glynn; Michael R Sawaya; David Eisenberg; Victor S Batista; Nikhil S Malvankar
Journal:  Proc Natl Acad Sci U S A       Date:  2021-01-12       Impact factor: 11.205

2.  Amyloid Fibrils from Hemoglobin.

Authors:  Nadishka Jayawardena; Manmeet Kaur; Smitha Nair; Jenny Malmstrom; David Goldstone; Leonardo Negron; Juliet A Gerrard; Laura J Domigan
Journal:  Biomolecules       Date:  2017-04-11

3.  Insights into the Origin of Distinct Medin Fibril Morphologies Induced by Incubation Conditions and Seeding.

Authors:  Hannah A Davies; Chiu Fan Lee; Leanne Miller; Lu-Ning Liu; Jillian Madine
Journal:  Int J Mol Sci       Date:  2018-05-03       Impact factor: 5.923

4.  Molecular dynamics simulations of mechanical failure in polymorphic arrangements of amyloid fibrils containing structural defects.

Authors:  Hlengisizwe Ndlovu; Alison E Ashcroft; Sheena E Radford; Sarah A Harris
Journal:  Beilstein J Nanotechnol       Date:  2013-07-04       Impact factor: 3.649

5.  Study of Nanofibrils Formation of Fibroin Protein in Specific Thermal and Acidity Conditions.

Authors:  Ahrami M; Khatami M; Heli H
Journal:  J Biomed Phys Eng       Date:  2020-02-01
  5 in total

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