Textiles, Merchandising and Fashion Design, Department of

 

Date of this Version

2014

Citation

RSC Adv., 2014, 4, 15451; DOI: 10.1039/c3ra47547f

Comments

Copyright The Royal Society of Chemistry 2014

Abstract

Soy protein, the plant protein from soybean, was electrospun into intrinsically water-stable scaffolds with large volume and ultrafine fibers oriented randomly and evenly in three dimensions (3D) to simulate native extracellular matrices of soft tissues. The 3D ultrafine fibrous scaffolds from proteins could be favored in soft tissue engineering. However, protein-based biomaterials usually suffered from poor water stability, while the highly cross-linked proteins which had water stability were usually difficult to be fabricated into fibers. Soy protein was a typical protein with intrinsic water stability, attributed to its 1.2% cysteine content. Soy protein has been developed into 3D non-fibrous structures, coarse fibers and films for tissue engineering applications, but not ultrafine fibrous structures. In this research, the disulfide crosslinks in soy protein were cleaved to facilitate its dissolution in an aqueous solvent system. The obtained solution was electrospun into bulky scaffolds composed of ultrafine fibers oriented randomly in three dimensions. Without external crosslinking, the fibrous soy protein scaffolds demonstrated long-term water stability, and maintained their fibrous structures after incubated in PBS for up to 28 days. In vitro study showed that the 3D soy protein scaffolds well supported uniform distribution and adipogenic differentiation of adipose derived mesenchymal stem cells. In summary, the 3D ultrafine fibrous soy protein structures could be good candidates as scaffolds in soft tissue engineering.

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