Next Article in Journal / Special Issue
Diversity of Amyloid Motifs in NLR Signaling in Fungi
Previous Article in Journal
QueF-Like, a Non-Homologous Archaeosine Synthase from the Crenarchaeota
Article Menu

Export Article

Open AccessArticle
Biomolecules 2017, 7(2), 37;

Amyloid Fibrils from Hemoglobin

School of Biological Sciences, The University of Auckland, Auckland 1010, New Zealand
School of Biological Sciences, University of Canterbury, Christchurch 8041, New Zealand
Department of Chemical and Materials Engineering, The University of Auckland, Auckland 1010, New Zealand
The MacDiarmid Institute for Advanced Materials and Nanotechnology, Wellington 6140, New Zealand
Callaghan Innovation, Lower Hutt 2010, New Zealand
School of Chemical Sciences, The University of Auckland, Auckland 1010, New Zealand
Author to whom correspondence should be addressed.
Academic Editors: Matthew Chapman, Daniel Otzen and Sarah Perrett
Received: 11 January 2017 / Revised: 16 March 2017 / Accepted: 5 April 2017 / Published: 11 April 2017
(This article belongs to the Special Issue Functional Amyloids)
Full-Text   |   PDF [7795 KB, uploaded 13 April 2017]   |  


Amyloid fibrils are a class of insoluble protein nanofibers that are formed via the self-assembly of a wide range of peptides and proteins. They are increasingly exploited for a broad range of applications in bionanotechnology, such as biosensing and drug delivery, as nanowires, hydrogels, and thin films. Amyloid fibrils have been prepared from many proteins, but there has been no definitive characterization of amyloid fibrils from hemoglobin to date. Here, nanofiber formation was carried out under denaturing conditions using solutions of apo-hemoglobin extracted from bovine waste blood. A characteristic amyloid fibril morphology was confirmed by transmission electron microscopy (TEM) and atomic force microscopy (AFM), with mean fibril dimensions of approximately 5 nm diameter and up to several microns in length. The thioflavin T assay confirmed the presence of β-sheet structures in apo-hemoglobin fibrils, and X-ray fiber diffraction showed the characteristic amyloid cross-β quaternary structure. Apo-hemoglobin nanofibers demonstrated high stability over a range of temperatures (−20 to 80 °C) and pHs (2–10), and were stable in the presence of organic solvents and trypsin, confirming their potential as nanomaterials with versatile applications. This study conclusively demonstrates the formation of amyloid fibrils from hemoglobin for the first time, and also introduces a cost-effective method for amyloid fibril manufacture using meat industry by-products. View Full-Text
Keywords: amyloid fibrils; hemoglobin; nanofiber; nanofibril amyloid fibrils; hemoglobin; nanofiber; nanofibril

Graphical abstract

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

Supplementary material


Share & Cite This Article

MDPI and ACS Style

Jayawardena, N.; Kaur, M.; Nair, S.; Malmstrom, J.; Goldstone, D.; Negron, L.; Gerrard, J.A.; Domigan, L.J. Amyloid Fibrils from Hemoglobin. Biomolecules 2017, 7, 37.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Biomolecules EISSN 2218-273X Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top