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Protein Microgels from Amyloid Fibril Networks

  • Lianne W. Y. Roode
  • Ulyana ShimanovichEmail author
  • Si Wu
  • Sarah PerrettEmail author
  • Tuomas P. J. KnowlesEmail author
Chapter
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 1174)

Abstract

Nanofibrillar forms of amyloidogenic proteins were initially discovered in the context of protein misfolding and disease but have more recently been found at the origin of key biological functionality in many naturally occurring functional materials, such as adhesives and biofilm coatings. Their physiological roles in nature reflect their great strength and stability, which has led to the exploration of their use as the basis of artificial protein-based functional materials. Particularly for biomedical applications, they represent attractive building blocks for the development of, for instance, drug carrier agents due to their inherent biocompatibility and biodegradability. Furthermore, the propensity of proteins to self-assemble into amyloid fibrils can be exploited under microconfinement, afforded by droplet microfluidic techniques. This approach allows the generation of multi-scale functional microgels that can host biological additives and can be designed to incorporate additional functionality, such as to aid targeted drug delivery.

Keywords

Self-assembled amyloid fibrils Protein microgels Droplet microfluidics Drug carrier agents Functional materials 

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Copyright information

© Springer Nature Singapore Pte Ltd. 2019

Authors and Affiliations

  1. 1.Centre for Misfolding Diseases, Department of ChemistryUniversity of CambridgeCambridgeUK
  2. 2.Department of Materials and InterfacesWeizmann Institute of ScienceRehovotIsrael
  3. 3.National Laboratory of Biomacromolecules, CAS Center for Excellence in BiomacromoleculesInstitute of Biophysics, Chinese Academy of SciencesBeijingChina
  4. 4.University of the Chinese Academy of SciencesBeijingChina
  5. 5.Cavendish Laboratory, University of CambridgeCambridgeUK

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