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Large and small assembly: combining functional macromolecules with small peptides to control the morphology of skeletal muscle progenitor cells

journal contribution
posted on 12.03.2018, 00:00 authored by Rui Li, Natasha McraeNatasha Mcrae, Daniel Mcculloch, Mitchell Boyd-Moss, Colin BarrowColin Barrow, D R Nisbet, Nicole Stupka, R J Williams
The material properties of natural tissues, such as skeletal muscle, are highly sophisticated and are synthetically challenging to mimic. Using natural biomacromolecules to functionalize self-assembled peptide (SAP) hydrogels has the potential to increase the utility of these materials by more closely reproducing the natural cellular environment. Here, to demonstrate that a conserved co-assembly pathway can retain distinct function, the biocompatible peptide derivative Fmoc-FRGDF was co-assembled with either a sulfated polysaccharide, fucoidan, or the provisional matrix proteoglycan, versican. Our results demonstrate that thermodynamically driven co-assembly with biologically active macromolecules is facile, stable, and does not affect the final assembled nanostructure. Biologically, the incorporation of these functionally distinct molecules had no effect on C2C12 myoblast proliferation and viability but strongly altered their morphology. The surface area of myoblasts cultured on the fucoidan scaffold was reduced at 24 and 72 h post seeding, with a reduction in the formation of multinucleated syncytia. Myoblasts cultured on versican scaffolds were smaller compared to cells grown on the empty vector scaffolds at 24 h but not 72 h post seeding, with multinucleated syncytia formation being unaffected. This work allows programmed and distinct morphological effects of cell behavior, paving the way for further mechanistic studies.

History

Journal

Biomacromolecules

Volume

19

Issue

3

Pagination

825 - 837

Publisher

American Chemical Society

Location

Washington, D.C.

ISSN

1525-7797

eISSN

1526-4602

Language

eng

Publication classification

C Journal article; C1 Refereed article in a scholarly journal

Copyright notice

2018, American Chemical Society