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Amyloids and their untapped potential as hydrogelators.

Vinay Kumar Belwal1, Nitin Chaudhary

  • 1Department of Biosciences and Bioengineering, Indian Institute of Technology Guwahati, Guwahati - 781 039, India. chaudhary@iitg.ac.in.

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Amyloid fibrils, once thought pathogenic, are now recognized as native structures. This discovery opens avenues for using amyloid hydrogels as biocompatible materials in diverse applications.

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Area of Science:

  • Biomaterials Science
  • Molecular Biology
  • Biochemistry

Background:

  • Amyloid fibrils are protein aggregates with a cross-β-sheet structure, historically linked to diseases.
  • Recent findings show that amyloid structures can be native and functional, with cytotoxicity attributed to pre-fibrillar species.
  • Functional amyloids are found across various organisms, from bacteria to humans.

Purpose of the Study:

  • To review the literature on amyloid hydrogels.
  • To discuss the potential applications of amyloid hydrogels.
  • To highlight the untapped potential of amyloids in material science.

Main Methods:

  • Literature review of studies on amyloidogenic proteins and peptides.
  • Analysis of research on hydrogel formation from amyloid structures.
  • Compilation of reported applications of amyloid hydrogels.

Main Results:

  • Amyloid fibrils are not inherently pathogenic and can be native structures.
  • Many amyloidogenic proteins and peptides can form hydrogels.
  • Amyloid hydrogels show promise for various applications, particularly in medicine.

Conclusions:

  • The cross-β-sheet motif is a native fold, not exclusively pathogenic.
  • Amyloid hydrogels represent a largely untapped resource for biocompatible materials.
  • Further research into amyloid hydrogels can lead to significant advancements in biomedical and other engineering fields.