TY - JOUR
T1 - Self-crosslinked gliadin fibers with high strength and water stability for potential medical applications
AU - Reddy, Narendra
AU - Yang, Yiqi
N1 - Funding Information:
Acknowledgements This research was partially supported with funds from Nebraska Wheat Board, The Consortium for Plant Biotechnology Research, Inc by DOE prime agreement No. DE-FG36-02G012026, Archer Daniel Midland Company, USDA Hatch Act, the Agricultural Research Division at the University of Nebraska-Lincoln and by Multi State Research Project S-1026. The financial sponsors do not endorse the views expressed in this publication. We also thank Dr. Liping Xie at the Veterinary Diagnostic Center for her help in the cell culture experiments and Ying Li for her help in the electrophoresis and water stability studies.
PY - 2008/5
Y1 - 2008/5
N2 - 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.
AB - 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.
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U2 - 10.1007/s10856-007-3294-0
DO - 10.1007/s10856-007-3294-0
M3 - Article
C2 - 17968503
AN - SCOPUS:41149111852
SN - 0957-4530
VL - 19
SP - 2055
EP - 2061
JO - Journal of Materials Science: Materials in Medicine
JF - Journal of Materials Science: Materials in Medicine
IS - 5
ER -