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Related Concept Videos

Amyloid Fibrils03:03

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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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Enzymatic Installation of Functional Molecules on Amyloid-Based Polymers.

Tatsuki Ohshima1, Masafumi Sakono1

  • 1Department of Applied Chemistry, Graduate School of Science and Engineering, University of Toyama , 3190 Gofuku, Toyama 930-8555, Japan.

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|October 26, 2017
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Summary

Researchers created a functional polymer using transthyretin (TTR) amyloid fibrils. They demonstrated that immobilized molecules can be detached and replaced using sortase A (srtA) enzyme, enabling dynamic functionalization of amyloid materials.

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Area of Science:

  • Biomaterials Science
  • Protein Engineering
  • Nanotechnology

Background:

  • Amyloid fibrils, derived from transthyretin (TTR), offer a unique structural framework for biomaterials.
  • Sortase A (srtA) is a transpeptidase enzyme capable of catalyzing covalent bond formation between specific peptide motifs (LPXTG and polyglycine).

Purpose of the Study:

  • To develop a functional polymer based on TTR amyloid fibrils.
  • To immobilize functional molecules, such as Green Fluorescent Protein (GFP), onto these amyloid fibrils.
  • To investigate the dynamic interchangeability of immobilized molecules on the amyloid scaffold.

Main Methods:

  • Preparation of TTR amyloid fibrils engineered with an LPETGG tag.
  • Immobilization of Gly5-fused GFP onto the TTR amyloid fibrils using srtA-mediated transpeptidation.
  • Demonstration of molecule exchange by replacing GFP with Gly5-fused luciferase using srtA.

Main Results:

  • Successful preparation of GFP-immobilized TTR amyloid fibrils, with srtA efficiently recognizing the tagged TTR variant.
  • Confirmation of dynamic molecule substitution: GFP was successfully detached and replaced by luciferase.
  • Demonstrated the ability to covalently immobilize, detach, and substitute functional molecules on amyloid fibrils.

Conclusions:

  • Functional polymers can be constructed using TTR amyloid fibrils as a scaffold.
  • srtA enzyme enables efficient and specific covalent immobilization of functional proteins onto amyloid structures.
  • The developed system allows for dynamic and reversible functionalization of amyloid-based materials.