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Related Experiment Videos

Amyloid Fibrils from Hemoglobin.

Nadishka Jayawardena1, Manmeet Kaur2, Smitha Nair3

  • 1School of Biological Sciences, The University of Auckland, Auckland 1010, New Zealand. gjay797@aucklanduni.ac.nz.

Biomolecules
|April 12, 2017
PubMed
Summary

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This summary is machine-generated.

Researchers have successfully created amyloid fibrils from hemoglobin, a novel protein nanomaterial. These stable hemoglobin nanofibers offer a cost-effective biomaterial for diverse nanotechnology applications.

Area of Science:

  • Biomaterials Science
  • Nanotechnology
  • Protein Chemistry

Background:

  • Amyloid fibrils are protein nanofibers with diverse applications in bionanotechnology.
  • While amyloid fibrils can be formed from various proteins, hemoglobin-derived fibrils have not been previously characterized.
  • Hemoglobin is abundant and available as a by-product of the meat industry.

Purpose of the Study:

  • To characterize amyloid fibrils formed from apo-hemoglobin.
  • To investigate the stability and potential applications of hemoglobin-derived amyloid fibrils.

Main Methods:

  • Apo-hemoglobin was extracted from bovine waste blood and subjected to denaturing conditions to induce nanofiber formation.
  • Transmission electron microscopy (TEM) and atomic force microscopy (AFM) were used to analyze fibril morphology.
Keywords:
amyloid fibrilshemoglobinnanofibernanofibril

Related Experiment Videos

  • Thioflavin T assay and X-ray fiber diffraction confirmed the presence of β-sheet structures and cross-β quaternary structure.
  • Stability was tested across various temperatures, pH levels, organic solvents, and enzymatic conditions.

    • Main Results:

    • Characteristic amyloid fibril morphology was observed, with mean dimensions of approximately 5 nm diameter and several microns in length.
    • The thioflavin T assay and X-ray fiber diffraction confirmed the presence of amyloidogenic β-sheet structures.
    • Apo-hemoglobin nanofibers exhibited high stability across a wide range of temperatures (-20 to 80 °C) and pH (2-10).
    • Fibrils remained stable in organic solvents and in the presence of trypsin.

    Conclusions:

    • This study provides the first definitive characterization of amyloid fibrils formed from hemoglobin.
    • The findings demonstrate a novel, cost-effective method for producing amyloid fibrils from readily available hemoglobin by-products.
    • Hemoglobin-derived amyloid fibrils possess remarkable stability, indicating significant potential for versatile applications in nanomaterials and bionanotechnology.