This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at firstname.lastname@example.org
Controlling the dimensions of amyloid fibrils: Toward homogenous components for bionanotechnology†
Article first published online: 19 AUG 2011
Copyright © 2011 Wiley Periodicals, Inc.
Volume 97, Issue 2, pages 123–133, February 2012
How to Cite
Domigan, L. J., Healy, J. P., Meade, S. J., Blaikie, R. J. and Gerrard, J. A. (2012), Controlling the dimensions of amyloid fibrils: Toward homogenous components for bionanotechnology. Biopolymers, 97: 123–133. doi: 10.1002/bip.21709
- Issue published online: 23 NOV 2011
- Article first published online: 19 AUG 2011
- Manuscript Accepted: 20 JUL 2011
- Manuscript Revised: 5 JUL 2011
- Manuscript Received: 4 MAY 2011
- MacDiarmid Institute for Advanced Materials
- amyloid fibrils;
- protein structures
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. © 2011 Wiley Periodicals, Inc. Biopolymers 97: 123–133, 2012.