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The ZT biopolymer: a self-assembling protein scaffold for stem cell applications

Nesterenko, Yevheniia, Hill, Christopher J., Fleming, Jennifer R., Murray, Patricia, Mayans, Olga·2019·International Journal of Molecular Sciences
DOI 10.3390/ijms20174299PMC PMC6747707
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Abstract

The development of cell culture systems for the naturalistic propagation, self-renewal and differentiation of cells ex vivo is a high goal of molecular engineering. Despite significant success in recent years, the high cost of up-scaling cultures, the need for xeno-free culture conditions, and the degree of mimicry of the natural extracellular matrix attainable in vitro using designer substrates continue to pose obstacles to the translation of cell-based technologies. In this regard, the ZT biopolymer is a protein-based, stable, scalable, and economical cell substrate of high promise. ZT is based on the naturally occurring assembly of two human proteins: titin-Z1Z2 and telethonin. These protein building blocks are robust scaffolds that can be conveniently functionalized with full-length proteins and bioactive peptidic motifs by genetic manipulation, prior to self-assembly. The polymer is, thereby, fully encodable. Functionalized versions of the ZT polymer have been shown to successfully sustain the long-term culturing of human embryonic stem cells (hESCs), human induced pluripotent stem cells (hiPSCs), and murine mesenchymal stromal cells (mMSCs). Pluripotency of hESCs and hiPSCs was retained for the longest period assayed (4 months). Results point to the large potential of the ZT system for the creation of a modular, pluri-functional biomaterial for cell-based applications.

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Authors
Nesterenko, Y., Hill, C. J., Fleming, J. R., Murray, P., & Mayans, O.
Affiliations
  • Department of Biology, University of Konstanz, 78457 Konstanz, Germany
  • Department of Cellular and Molecular Physiology, Institute of Translational Medicine, University of Liverpool, Liverpool L69 3BX, UK
ORCID
Venue
International Journal of Molecular Sciences
Publisher
MDPI AG
Published
2019-09-03
Volume
20
Issue
17
Pages
4299
ISSN
1422-0067
DOI
10.3390/ijms20174299
PMC
PMC6747707
Cited by
5
References
1
Language
en
Licence
creativecommons.org/licenses/by/4.0/ (vor)
Funders
  • BBSRC (-)
  • Konstanz Research School of Chemical Biology (-)
  • The Welcome Trust (204401/z/16/z)
  • EU Marie Sklodowska-­Curie (TTNPred, 753054)

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