Water-Stable Silk Films with Reduced β-Sheet Content

Advanced Functional MaterialsVolume 15, Issue 8 p. 1241-1247 Full Paper Water-Stable Silk Films with Reduced β-Sheet Content† H.-J. Jin, H.-J. Jin Department of Polymer Science and Engineering, Inha University, Incheon 402–751, KoreaSearch for more papers by this authorJ. Park, J. Park Departments of Biomedical Engineering, Chemical & Biological Engineering, and Physics and Astronomy, Tufts University, Medford, MA 02155, USASearch for more papers by this authorV. Karageorgiou, V. Karageorgiou Departments of Biomedical Engineering, Chemical & Biological Engineering, and Physics and Astronomy, Tufts University, Medford, MA 02155, USASearch for more papers by this authorU.-J. Kim, U.-J. Kim Departments of Biomedical Engineering, Chemical & Biological Engineering, and Physics and Astronomy, Tufts University, Medford, MA 02155, USASearch for more papers by this authorR. Valluzzi, R. Valluzzi Departments of Biomedical Engineering, Chemical & Biological Engineering, and Physics and Astronomy, Tufts University, Medford, MA 02155, USASearch for more papers by this authorP. Cebe, P. Cebe Departments of Biomedical Engineering, Chemical & Biological Engineering, and Physics and Astronomy, Tufts University, Medford, MA 02155, USASearch for more papers by this authorD. L. Kaplan, D. L. Kaplan david.kaplan@tufts.edu Departments of Biomedical Engineering, Chemical & Biological Engineering, and Physics and Astronomy, Tufts University, Medford, MA 02155, USASearch for more papers by this author H.-J. Jin, H.-J. Jin Department of Polymer Science and Engineering, Inha University, Incheon 402–751, KoreaSearch for more papers by this authorJ. Park, J. Park Departments of Biomedical Engineering, Chemical & Biological Engineering, and Physics and Astronomy, Tufts University, Medford, MA 02155, USASearch for more papers by this authorV. Karageorgiou, V. Karageorgiou Departments of Biomedical Engineering, Chemical & Biological Engineering, and Physics and Astronomy, Tufts University, Medford, MA 02155, USASearch for more papers by this authorU.-J. Kim, U.-J. Kim Departments of Biomedical Engineering, Chemical & Biological Engineering, and Physics and Astronomy, Tufts University, Medford, MA 02155, USASearch for more papers by this authorR. Valluzzi, R. Valluzzi Departments of Biomedical Engineering, Chemical & Biological Engineering, and Physics and Astronomy, Tufts University, Medford, MA 02155, USASearch for more papers by this authorP. Cebe, P. Cebe Departments of Biomedical Engineering, Chemical & Biological Engineering, and Physics and Astronomy, Tufts University, Medford, MA 02155, USASearch for more papers by this authorD. L. Kaplan, D. L. Kaplan david.kaplan@tufts.edu Departments of Biomedical Engineering, Chemical & Biological Engineering, and Physics and Astronomy, Tufts University, Medford, MA 02155, USASearch for more papers by this author First published: 01 July 2005 https://doi.org/10.1002/adfm.200400405Citations: 485 † We thank the NIH (R01 DE13405–04, R01EB003210–02), the NSF (DMR-0090384), and the DoD (Air Force) for support of this program. Cocoons of B. mori silkworm silk were kindly supplied by M. Tsukada, Institute of Sericulture, Tsukuba, Japan. AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Abstract Silk fibers have outstanding mechanical properties. These fibers are insoluble in organic solvents and water, are biocompatible, and exhibit slow biodegradation in vitro and in vivo due to the hydrophobic nature of the protein and the presence of a high content of β-sheet structure. Regenerated silk fibroin can be processed into a variety of materials normally stabilized by the induction of β-sheet formation through the use of solvents or by physical stretching. To extend the biomaterial utility of silk proteins, options to form water-stable silk-based materials with reduced β-sheet formation would be desirable. To address this need for more rapidly degradable silk biomaterials, we report the preparation of water-stable films from regenerated silk fibroin solutions, with reduced β-sheet content. The keys to this process are the preparation of concentrated (8 % by weight) aqueous solutions of fibroin and a subsequent water-based annealing procedure. These new materials degrade more rapidly due to the reduced β-sheet content, as determined in vitro via enzymatic hydrolysis, yet support human adult stem-cell expansion in vitro in a similar or improved fashion to the crystallized proteins in film form. These new silk-based materials extend the range of biomaterial properties that can be generated from this unique family of proteins. Citing Literature Volume15, Issue8August, 2005Pages 1241-1247 RelatedInformation