Abstract
Silk fibroin materials can be used as various kinds of biomedical materials. Here, we report a comparative study of silk-silk blend materials using thermal analysis and infrared spectroscopy. Four groups of silk-silk blend films were fabricated from aqueous solutions by blending Chinese Bombyx mori (Mori) with Indian Antheraea mylitta (Tussah) silk fibroin (Mori-Tussah), Mori with Antheraea assama (Muga) silk fibroin (Mori-Muga), Mori with Philosamia ricini (Eri) silk fibroin (Mori-Eri), and Mori with Thailand mulberry (Thai) silk fibroin (Mori-Thai), respectively. These silk-silk blend systems exploit the beneficial material properties of both silks. Glass transition temperatures (T g), heat capacity increments at T g, and degradation temperatures (T d) of these water-based silk-silk blend films were measured by differential scanning calorimetry (DSC) and temperature-modulated DSC (TMDSC). It was found that those silk-silk film systems were well-blended without macrophase separation. And glass transition temperatures and degradation temperatures of those silk-silk blend films can be controlled by changing the mass ratio of different silks in the blend system. Fourier transform infrared spectrometer (FTIR) was used to characterize secondary structures of silk-silk blends. The contents of alpha-helix and random coils are tunable through changing the contents of Tussah, Muga, Eri, or Thai silk in the blend system. The study demonstrates that Mori silk are fully miscible with Tussah, Muga, Eri, and Thai silk at different mass ratios, and the features of Mori silk combined with the attributes of Tussah, Muga, Eri, and Thai silk offer a useful suite of materials for a variety of applications in the future.
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References
Kaplan D, McGrath K. Protein-based materials. Berlin: Springer Science & Business Media; 2012.
Ha S-W, Gracz HS, Tonelli AE, Hudson SM. Structural study of irregular amino acid sequences in the heavy chain of bombyx Mori silk fibroin. Biomacromolecules. 2005;6(5):2563–9.
Jin H-J, Kaplan DL. Mechanism of silk processing in insects and spiders. Nature. 2003;424(6952):1057–61.
Heinz A, Jung MC, Duca L, Sippl W, Taddese S, Ihling C, et al. Degradation of tropoelastin by matrix metalloproteinases–cleavage site specificities and release of matrikines. FEBS J. 2010;277(8):1939–56.
Hu X, Lu Q, Sun L, Cebe P, Wang X, Zhang X, et al. Biomaterials from ultrasonication-induced silk fibroin—hyaluronic acid hydrogels. Biomacromolecules. 2010;11(11):3178–88.
Omenetto FG, Kaplan DL. New opportunities for an ancient material. Science. 2010;329(5991):528–31.
Zhang J, Rajkhowa R, Li J, Liu X, Wang X. Silkworm cocoon as natural material and structure for thermal insulation. Mater Des. 2013;49:842–9.
Hu X, Wang X, Rnjak J, Weiss AS, Kaplan DL. Biomaterials derived from silk–tropoelastin protein systems. Biomaterials. 2010;31(32):8121–31.
Cebe P, Hu X, Kaplan DL, Zhuravlev E, Wurm A, Arbeiter D et al. Beating the heat-fast scanning melts silk beta sheet crystals. Scientific reports. 2013;3.
Wang X, Yucel T, Lu Q, Hu X, Kaplan DL. Silk nanospheres and microspheres from silk/pva blend films for drug delivery. Biomaterials. 2010;31(6):1025–35.
Hu X, Cebe P, Weiss AS, Omenetto F, Kaplan DL. Protein-based composite materials. Mater Today. 2012;15(5):208–15.
Ekemen Z, Ahmad Z, Stride E, Kaplan D, Edirisinghe M. Electrohydrodynamic bubbling: an alternative route to fabricate porous structures of silk fibroin based materials. Biomacromolecules. 2013;14(5):1412–22.
Miwa Y, Usami K, Yamamoto K, Sakaguchi M, Sakai M, Shimada S. Direct detection of effective glass transitions in miscible polymer blends by temperature-modulated differential scanning calorimetry. Macromolecules. 2005;38(6):2355–61.
Park S-H, Gil ES, Shi H, Kim HJ, Lee K, Kaplan DL. Relationships between degradability of silk scaffolds and osteogenesis. Biomaterials. 2010;31(24):6162–72.
Kim U-J, Park J, Kim HJ, Wada M, Kaplan DL. Three-dimensional aqueous-derived biomaterial scaffolds from silk fibroin. Biomaterials. 2005;26(15):2775–85.
Kim U-J, Park J, Li C, Jin H-J, Valluzzi R, Kaplan DL. Structure and properties of silk hydrogels. Biomacromolecules. 2004;5(3):786–92.
Motta A, Maniglio D, Migliaresi C, Kim H-J, Wan X, Hu X, et al. Silk fibroin processing and thrombogenic responses. J Biomater Sci Polym Ed. 2009;20(13):1875–97.
Mazzi S, Zulker E, Buchicchio J, Anderson B, Hu X. Comparative thermal analysis of Eri, Mori, Muga, and Tussar silk cocoons and fibroin fibers. J Therm Anal Calorim. 2014;116(3):1337–43.
Wang F, Wolf N, Rocks E-M, Vuong T, Hu X. Comparative studies of regenerated water-based Mori, Thai, Eri, Muga and Tussah silk fibroin films. J Therm Anal Calorim. 2015;122(3):1069–1076.
Pyda M, Hu X, Cebe P. Heat capacity of silk fibroin based on the vibrational motion of poly (amino acid) s in the presence and absence of water. Macromolecules. 2008;41(13):4786–93.
Hu X, Park S-H, Gil ES, Xia X-X, Weiss AS, Kaplan DL. The influence of elasticity and surface roughness on myogenic and osteogenic-differentiation of cells on silk-elastin biomaterials. Biomaterials. 2011;32(34):8979–89.
Wunderlich B, Jin Y, Boller A. Mathematical description of differential scanning calorimetry based on periodic temperature modulation. Thermochim Acta. 1994;238:277–93.
Boller A, Okazaki I, Ishikiriyama K, Zhang G, Wunderlich B. Determination of cell asymmetry in temperature-modulated DSC. J Therm Anal Calorim. 1997;49(2):1081–8.
Mao B, Cebe P. Avrami analysis of melt crystallization behavior of Trogamid. J Therm Anal Calorim. 2013;113(2):545–50.
Xu H, Cebe P. Heat capacity study of isotactic polystyrene: dual reversible crystal melting and relaxation of rigid amorphous fraction. Macromolecules. 2004;37(8):2797–806.
Barth A. Infrared spectroscopy of proteins. Biochim Biophys Acta (BBA) Bioenergetics. 2007;1767(9):1073–101.
Barth A, Zscherp C. What vibrations tell about proteins. Q Rev Biophys. 2002;35(04):369–430.
Jung C. Insight into protein structure and protein–ligand recognition by Fourier transform infrared spectroscopy. J Mol Recognit. 2000;13(6):325–51.
Hu X, Shmelev K, Sun L, Gil E-S, Park S-H, Cebe P, et al. Regulation of silk material structure by temperature-controlled water vapor annealing. Biomacromolecules. 2011;12(5):1686–96.
Hu X, Kaplan D, Cebe P. Determining beta-sheet crystallinity in fibrous proteins by thermal analysis and infrared spectroscopy. Macromolecules. 2006;39(18):6161–70.
Acknowledgements
The authors would like to thank Nathan Wolf and Eva-Marie Rocks for their support and assistance with this project. This study was supported by the Rowan University Start-up Grants, NSF-MRI Program (DMR-1338014), and New Jersey Space Grant Consortium.
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Xue, Y., Jao, D., Hu, W. et al. Silk-silk blend materials. J Therm Anal Calorim 127, 915–921 (2017). https://doi.org/10.1007/s10973-016-5699-9
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DOI: https://doi.org/10.1007/s10973-016-5699-9