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Lookup NU author(s): Dr Gema Dura, Dr Daniel PetersORCiD, Dr Helen WallerORCiD, Dr Adrian Yemm, Professor Neil PerkinsORCiD, Dr Ana Ferreira-DuarteORCiD, Dr Maria Crespo Cuadrado, Professor Jeremy LakeyORCiD, Professor David Fulton
This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License (CC BY-NC-ND).
Complex biomaterials easily formed by self-assembling proteins could transform regenerative medicine and 3D cell culture. However, while readily achieved by short peptides, materials assembled from proteins with defined tertiary structure are still rare. The bacterial fimbrial protein, capsular antigen fragment 1 (Caf1), forms long polymers of subunits linked by kinetically stable non-covalent interactions which can be further chemically crosslinked into a variety of hydrogels. We report here that the complete thermal dissociation of Caf1 polymers or hydrogels into individual subunits is fully reversible with high yield. This simple feature endows the Caf1 polymer with outstanding synthetic and materials possibilities and, to demonstrate, we describe the in vitro assembly of complex bioactive copolymers and provide example applications of meltable protein hydrogels. We anticipate that the highly efficient and reversible assembly of these multifunctional polymeric proteins will enhance significantly the development of proteinaceous biomaterials for clinical and industrial applications.
Author(s): Dura G, Peters DT, Waller H, Yemm AI, Perkins ND, Ferreira AM, Crespo-Cuadrado M, Lakey JH, Fulton DA
Publication type: Article
Publication status: Published
Journal: Chem
Year: 2020
Volume: 6
Issue: 11
Pages: 3132-3151
Print publication date: 05/11/2020
Online publication date: 21/10/2020
Acceptance date: 23/09/2020
Date deposited: 12/11/2020
ISSN (print): 2451-9308
ISSN (electronic): 2451-9294
Publisher: Cell Press
URL: https://doi.org/10.1016/j.chempr.2020.09.020
DOI: 10.1016/j.chempr.2020.09.020
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