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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
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Rapid Generation of Amyloid from Native Proteins In vitro
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Novel, Inexpensive, and Scalable Amyloid Fibril Formation Method.

Ethan Hessick1, Milind Pawar1, Reid Souchereau1

  • 1Advanced Ceramics Research Laboratory, Department of Materials Science and Engineering, The Ohio State University, Columbus, OH 43210, USA.

Materials (Basel, Switzerland)
|March 10, 2022
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Summary

Researchers developed a novel method to create amyloid fibrils from wheat flour protein for cost-effective nano-biomaterials. These amyloid fibers show potential for sensitive melatonin detection through color variation.

Keywords:
amyloidinexpensivemelatonin biosensingsynthesis

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Area of Science:

  • Biomaterials Science
  • Nanotechnology
  • Analytical Chemistry

Background:

  • Amyloid fibrils are protein aggregates with unique self-assembling properties.
  • Developing cost-effective and scalable methods for amyloid fibril synthesis is crucial for their application.
  • Wheat flour is an abundant and inexpensive protein source.

Purpose of the Study:

  • To establish a novel, inexpensive in vitro method for synthesizing amyloid fibrils using wheat flour protein.
  • To characterize the morphology and properties of the synthesized amyloid fibrils.
  • To explore the application of these novel amyloid fibrils in melatonin sensing.

Main Methods:

  • In vitro synthesis of amyloid fibrils from wheat flour protein.
  • Confirmation of fibrillation using Thioflavin T fluorescence and confocal microscopy.
  • Morphological analysis via transmission electron microscopy (TEM).
  • Evaluation of amyloid fibril application in melatonin sensing through colorimetric analysis.

Main Results:

  • Successful in vitro synthesis of amyloid fibrils from wheat flour protein.
  • Amyloid fibrils exhibited a high aspect ratio as observed by TEM.
  • The synthesized amyloid fibers demonstrated measurable color changes in response to varying melatonin concentrations, indicating sensing capability.

Conclusions:

  • A novel and cost-effective method for producing amyloid fibrils from wheat flour protein has been developed.
  • The synthesized amyloid fibrils possess suitable morphology for nano-biomaterial applications.
  • This process offers a promising platform for developing affordable melatonin biosensors for research and commercial use.