Self-crosslinked gliadin fibers with high strength and water stability for potential medical applications

Abstract

For the first time, protein fibers with excellent mechanical properties and water stability have been produced from gliadin for potential use in tissue culture and other medical applications. Biomaterials developed from plant proteins such as zein and soyproteins are preferred for several medical applications over synthetic polymers such as polylactic acid. However, the plant protein based biomaterials developed so far have poor mechanical properties and hydrolytic stability even after crosslinking. This study aims to develop biomaterials from gliadin with excellent mechanical properties and water stability without using any crosslinking agents. A novel gliadin fiber production method was used to self crosslink the fibers and obtain high strength and water stability. Gliadin fibers have high strength (120 MPa) and elongation (25%) compared to similar collagen fibers that were crosslinked with glutaraldehyde (strength of about 44 MPa and elongation of 14%). The fibers show 100% strength retention after being in pH 7 water at 50 °C for 40 days and also have better water stability than PLA in acidic conditions at high temperatures. Gliadin fibers are suitable for cell growth and promote the attachment and proliferation of bovine turbinate fibroblasts.

Structure and properties of cocoons and silk fibers produced by Hyalophora cecropia

“…Therefore, efforts have been made since 1930s to produce regenerated protein fibers using various protein sources. Soyproteins, wheat gluten and gliadin, zein, keratin in feathers are some of the sources used to develop regenerated protein fibers [4][5][6]. Our group has demonstrated that byproducts such as soyprotein, zein, and wheat gluten obtained during processing of food grains for food and biofuels can be used to develop high quality regenerated protein fibers [4][5][6].…”

“…Soyproteins, wheat gluten and gliadin, zein, keratin in feathers are some of the sources used to develop regenerated protein fibers [4][5][6]. Our group has demonstrated that byproducts such as soyprotein, zein, and wheat gluten obtained during processing of food grains for food and biofuels can be used to develop high quality regenerated protein fibers [4][5][6]. The regenerated protein fibers developed from wheat gluten and soyproteins were crosslinked with carboxylic acids and reported to have properties similar to wool and suitable for textile and medical applications [7,8].…”

Developing Water Stable Gliadin Films Without Using Crosslinking Agents

“…In addition to films, plant proteins have also been used to develop regenerated protein fibers for various applications [6][7][8][9]. However, films and fibers made from plant proteins have relatively poor mechanical properties and stability in water compared to similar materials made from synthetic polymers.…”

“…The higher molecular weight gliadin proteins will have better mechanical properties and water stability compared to similar materials made from low molecular weight gliadin proteins. We have recently developed high quality protein fibers from gliadin using aqueous urea and sodium sulfite [9]. The intermolecular transformation of disulfide bonds in gliadin proteins in high concentration urea solutions provided excellent mechanical properties and water stability to the gliadin fibers [9].…”

“…We have recently developed high quality protein fibers from gliadin using aqueous urea and sodium sulfite [9]. The intermolecular transformation of disulfide bonds in gliadin proteins in high concentration urea solutions provided excellent mechanical properties and water stability to the gliadin fibers [9]. Attempts in our laboratory to develop gliadin films using the method used to produce the fibers were unsuccessful since the high concentrations of urea (8 M) used precipitated upon drying and could not be removed without disrupting the films.…”