Hostname: page-component-cd9895bd7-dzt6s Total loading time: 0 Render date: 2024-12-27T06:53:47.815Z Has data issue: false hasContentIssue false
  • English
  • Français

Assessing the influence of silkworm cocoon’s age on the physicochemical properties of silk fibroin-based materials

Published online by Cambridge University Press:  03 May 2019

Silvia Marisol Valles Ramirez ,
Mariana Agostini de Moraes Open the ORCID record for Mariana Agostini de Moraes [Opens in a new window]  and
Marisa Masumi Beppu
Silvia Marisol Valles Ramirez
Affiliation:
School of Chemical Engineering, Department of Materials and Bioprocess Engineering, University of Campinas, Campinas, SP 13083-852, Brazil
Mariana Agostini de Moraes
Affiliation:
Environmental, Chemical and Pharmaceutical Sciences Institute, Department of Chemical Engineering, Universidade Federal de São Paulo, Diadema, SP 09913-030, Brazil
Marisa Masumi Beppu*
Affiliation:
School of Chemical Engineering, Department of Materials and Bioprocess Engineering, University of Campinas, Campinas, SP 13083-852, Brazil
*
a)Address all correspondence to this author. e-mail: [email protected]
Get access

Abstract

The novelty of this study was to investigate for the first time in literature the influence of Bombyx mori silkworm cocoon’s age on the properties of silk fibroin-based materials, during all stages of cocoon processing to obtain the fibroin film. The study started with the premise that the cocoon age could cause modifications on fibroin properties during processing and, consequently, a possible interference on the characteristics of the final product. Characterizations were performed using batches of cocoons produced in different years, named C0 (fresh cocoons) and C6 (six-year-old cocoons). The influence of cocoon’s aging was observed on dialyzed dispersion regarding the molecular weight, particle size, and conformation. C6 films showed a more crystalline structure and higher thermal resistance than C0 films. The findings reported in this work are relevant for the reproducibility of fibroin-based materials, and the cocoon age is a key factor that should be considered in the preparation of fibroin-based materials.

Keywords

filmmacromolecular structuresolvent casting
Type
Article
Information
Journal of Materials Research , Volume 34 , Issue 11: Focus Issue: (Nano)materials for Biomedical Applications , 14 June 2019 , pp. 1944 - 1949
Copyright
Copyright © Materials Research Society 2019 

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Arai, T., Freddi, G., Innocenti, R., and Tsukada, M.: Biodegradation of Bombyx mori silk fibroin fibers and films. J. Appl. Polym. Sci. 91, 2383 (2004).CrossRefGoogle Scholar
Yucel, T., Lovett, M.L., and Kaplan, D.L.: Silk-based biomaterials for sustained drug delivery. J. Controlled Release 190, 381 (2014).CrossRefGoogle ScholarPubMed
Altman, G.H., Diaz, F., Jakuba, C., Calabro, T., Horan, R.L., Chen, J., Lu, H., Richmond, J., and Kaplan, D.L.: Silk-based biomaterials. Biomaterials 24, 401 (2003).CrossRefGoogle ScholarPubMed
Ki, C.S., Um, I.C., and Park, Y.H.: Acceleration effect of sericin on shear-induced β-transition of silk fibroin. Polymer 50, 4618 (2009).CrossRefGoogle Scholar
Kundu, B., Kurland, N.E., Bano, S., Patra, C., Engel, F.B., Yadavalli, V.K., and Kundu, S.C.: Silk proteins for biomedical applications: Bioengineering perspectives. Prog. Polym. Sci. 39, 251 (2014).CrossRefGoogle Scholar
Ahmed, H.E. and Darwish, S.S.: Effect of museum conditions on historical dyed silk fabric with madder dye. J. Polym. Environ. 20, 596 (2012).CrossRefGoogle Scholar
Koperska, M.A., Pawcenis, D., Bagniuk, J., Zaitz, M.M., Missori, M., Łojewski, T., and Łojewska, J.: Degradation markers of fibroin in silk through infrared spectroscopy. Polym. Degrad. Stab. 105, 185 (2014).CrossRefGoogle Scholar
Wang, Y., Rudym, D.D., Walsh, A., Abrahamsen, L., Kim, H-J., Kim, H.S., Kirker-Head, C., and Kaplan, D.L.: In vivo degradation of three-dimensional silk fibroin scaffolds. Biomaterials 29, 3415 (2008).CrossRefGoogle ScholarPubMed
Gong, D. and Yang, H.: The discovery of free radicals in ancient silk textiles. Polym. Degrad. Stab. 98, 1780 (2013).CrossRefGoogle Scholar
Koperska, M.A., Lojewski, T., and Lojewska, J.: Evaluating degradation of silk’s fibroin by attenuated total reflectance infrared spectroscopy: Case study of ancient banners from Polish collections. Spectrochim. Acta, Part A 135, 576 (2015).CrossRefGoogle ScholarPubMed
Mamedov, S.V., Akta, B., Cantürk, M., Aksakal, B., Alekperov, V., Bülbül, F., Yilgin, R., and Aslanov, R.B.: The ESR signals in silk fibroin and wool keratin under both the effect of UV-irradiation and without any external effects and the formation of free radicals. Biomaterials 23, 3405 (2002).CrossRefGoogle ScholarPubMed
Jin, H-J. and Kaplan, D.L.: Mechanism of silk processing in insects and spiders. Nature 424, 1057 (2003).CrossRefGoogle ScholarPubMed
Yamada, H., Nakao, H., Takasu, Y., and Tsubouchi, K.: Preparation of undegraded native molecular fibroin solution from silkworm cocoons. Mater. Sci. Eng., C 14, 41 (2001).CrossRefGoogle Scholar
Cheng, G., Wang, X., Tao, S., Xia, J., and Xu, S.: Differences in regenerated silk fibroin prepared with different solvent systems: From structures to conformational changes. J. Appl. Polym. Sci. 132, 41959 (2015).CrossRefGoogle Scholar
Lu, Q., Zhu, H., Zhang, C., Zhang, F., Zhang, B., and Kaplan, D.L.: Silk self-assembly mechanisms and control from thermodynamics to kinetics. Biomacromolecules 13, 826 (2012).CrossRefGoogle ScholarPubMed
Squier, T.C.: Oxidative stress and protein aggregation during biological aging. Exp. Gerontol. 36, 1539 (2001).CrossRefGoogle ScholarPubMed
Li, G., Zhou, P., Shao, Z., Xie, X., Chen, X., Wang, H., Chunyu, L., and Yu, T.: The natural silk spinning process. Eur. J. Biochem. 268, 6600 (2001).CrossRefGoogle ScholarPubMed
Um, I.C., Kweon, H., Park, Y.H., and Hudson, S.: Structural characteristics and properties of the regenerated silk fibroin prepared from formic acid. Int. J. Biol. Macromol. 29, 91 (2001).CrossRefGoogle ScholarPubMed