Abstract
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.
Highlights
Amyloid fibrils are highly organized, insoluble, fibrillar aggregates that are formed from a wide range of soluble peptides and proteins [1]
Amyloid fibrils were formed under the same conditions using hemoglobin extracted from bovine waste blood by red blood cell (RBC) lysis, which was purified to homogeneity, as described in the Methods section (Figure S1 and S2)
For 250 mL volumes, samples were incubated in a climatic chamber with an MB1 display controller (BINDER, GmbH, Tuttlingen, Germany). Driven by their high stability, mechanical properties, and ease of formation, amyloid fibrils have been investigated for numerous applications
Summary
Amyloid fibrils are highly organized, insoluble, fibrillar aggregates that are formed from a wide range of soluble peptides and proteins [1]. Previous research has demonstrated the functionalization of fibrils for various applications such as biosensors [9,10,11,12,13], nanowires [14,15,16], nanocomposites [17,18], thin films [19], nanoporous matrices [20], hydrogels [21], and aerogels [22].
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