Amyloid-Like Assembly to Form Film at Interfaces: Structural Transformation and Application

Macromol Biosci. 2023 Nov;23(11):e2300172. doi: 10.1002/mabi.202300172. Epub 2023 Jun 17.

Abstract

Protein-based biomaterials are attracting broad interest for their remarkable structural and functional properties. Disturbing the native protein's three-dimensional structural stability in vitro and controlling subsequent aggregation is an effective strategy to design and construct protein-based biomaterials. One of the recent developments in regulating protein structural transformation to ordered aggregation is amyloid assembly, which generates fibril-based 1D to 3D nanostructures as functional materials. Especially, the amyloid-like assembly to form films at interfaces has been reported, which is induced by the effective reduction of the intramolecular disulfide bond. The main contribution of this amyloid-like assembly is the large-scale formation of protein films at interfaces and excellent adhesion to target substrates. This review presents the research progress of the amyloid-like assembly to form films and related applications and thereby provides a guide to exploiting protein-based biomaterials.

Keywords: amyloid-like; folding and unfolding; protein films; surface/interface modifications.

Publication types

  • Review
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyloid* / chemistry
  • Amyloid* / metabolism
  • Biocompatible Materials*

Substances

  • Amyloid
  • Biocompatible Materials