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Collagen and elastin scaffold by electrospinning for skin tissue engineering applications

Published online by Cambridge University Press:  06 August 2019

Josué Jiménez Vázquez  and
Eduardo San Martín Martínez Open the ORCID record for Eduardo San Martín Martínez [Opens in a new window]
Josué Jiménez Vázquez
Affiliation:
Instituto Politécnico Nacional, Centro de Investigación en Ciencia Aplicada y Tecnología Avanzada, C.P. 11500 Ciudad de México, México
Eduardo San Martín Martínez*
Affiliation:
Instituto Politécnico Nacional, Centro de Investigación en Ciencia Aplicada y Tecnología Avanzada, C.P. 11500 Ciudad de México, México
*
a)Address all correspondence to this author. e-mail: esanmartin@ipn.mx
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Abstract

In recent years, tissue engineering has helped to reduce hospital stays and deaths caused by skin wounds. Scaffolds are one of the main factors that influence the success of any tissue graft. Collagen is one of the main components of the extracellular matrix, and there has been much interest in new sources for application as a biomaterial. In this work, a tissue engineering scaffold was developed using the electrospinning technique. The chicken skin was used as an alternative source to obtain collagen. The combination of this collagen with elastin was successfully electrospun, and a distribution of diameters was obtained, less than 100 nm. In vitro tests showed the adhesion and proliferation of the cells, as well as an absence of cytotoxicity from non–cross-linked scaffolds and scaffolds that were cross-linked with carbonyldiimidazole. The structure and composition of the developed scaffolding provide a favorable environment for cell growth and generating a skin substitute.

Keywords

scaffoldcollagenelectrospinningskintissue engineeringelastinbiomedicalbiomimetic (assembly)cellular

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Type
Article
Information
Journal of Materials Research , Volume 34 , Issue 16 , 28 August 2019 , pp. 2819 - 2827
Copyright
Copyright © Materials Research Society 2019 

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References

Hay, R.J., Augustin, M., Griffiths, C.E.M., Sterry, W., and Board of the International League of Dermatological Societies and the Grand Challenges Consultation Groups: The global challenge for skin health. Br. J. Dermatol. 172, 1469–1472 (2015).CrossRefGoogle ScholarPubMed
Vig, K., Chaudhari, A., Tripathi, S., Dixit, S., Sahu, R., Pillai, S., Dennis, V., and Singh, S.: Advances in skin regeneration using tissue engineering. Int. J. Mol. Sci. 18, 789 (2017).CrossRefGoogle ScholarPubMed
Park, Y.R., Ju, H.W., Lee, J.M., Kim, D-K., Lee, O.J., Moon, B.M., Park, H.J., Jeong, J.Y., Yeon, Y.K., and Park, C.H.: Three-dimensional electrospun silk-fibroin nanofiber for skin tissue engineering. Int. J. Biol. Macromol. 93, 1567–1574 (2016).CrossRefGoogle ScholarPubMed
Sundaramurthi, D., Krishnan, U.M., and Sethuraman, S.: Electrospun nanofibers as scaffolds for skin tissue engineering. Polym. Rev. 54, 348–376 (2014).CrossRefGoogle Scholar
Dias, J.R., Granja, P.L., and Bártolo, P.J.: Advances in electrospun skin substitutes. Prog. Mater. Sci. 84, 314–334 (2016).CrossRefGoogle Scholar
Ranjbarvan, P., Mahmoudifard, M., Kehtari, M., Babaie, A., Hamedi, S., Mirzaei, S., Soleimani, M., and Hosseinzadeh, S.: Natural compounds for skin tissue engineering by electrospinning of nylon-beta vulgaris. ASAIO J. 64, 261–269 (2018).CrossRefGoogle ScholarPubMed
Ramanathan, G., Singaravelu, S., Raja, M.D., Nagiah, N., Padmapriya, P., Ruban, K., Kaveri, K., Natarajan, T.S., Sivagnanam, U.T., and Perumal, P.T.: Fabrication and characterization of a collagen coated electrospun poly(3-hydroxybutyric acid)-gelatin nanofibrous scaffold as a soft bio-mimetic material for skin tissue engineering applications. RSC Adv. 6, 7914–7922 (2016).CrossRefGoogle Scholar
Chen, F-M. and Liu, X.: Advancing biomaterials of human origin for tissue engineering. Prog. Polym. Sci. 53, 86–168 (2016).CrossRefGoogle ScholarPubMed
Munasinghe, K.A., Schwarz, J.G., and Nyame, A.K.: Chicken collagen from law market value by-products as an alternate source. J. Food Process. 2015, 1 (2015).Google Scholar
Zhou, C., Li, Y., Yu, X., Yang, H., Ma, H., Yagoub, A.E.A., Cheng, Y., Hu, J., and Otu, P.N.Y.: Extraction and characterization of chicken feet soluble collagen. LWT–Food Sci. Technol. 74, 145–153 (2016).CrossRefGoogle Scholar
Cliche, S., Amiot, J., Avezard, C., and Gariepy, C.: Extraction and characterization of collagen with or without telopeptides from chicken skin. Poult. Sci. 82, 503–509 (2003).CrossRefGoogle ScholarPubMed
Gojkovic, Z., Marova, I., Matouskova, P., Obruca, S., and Miloslav, P.: Use of ultrasonic spectroscopy and viscosimetry for the characterization of chicken skin collagen in comparison with collagens from other animal tissues. Prep. Biochem. Biotechnol. 44, 761–771 (2014).CrossRefGoogle ScholarPubMed
Buttafoco, L., Kolkman, N.G., Engbers-Buijtenhuijs, P., Poot, A.A., Dijkstra, P.J., Vermes, I., and Feijen, J.: Electrospinning of collagen and elastin for tissue engineering applications. Biomaterials 27, 724–734 (2006).CrossRefGoogle ScholarPubMed
Rnjak-Kovacina, J., Wise, S.G., Li, Z., Maitz, P.K.M., Young, C.J., Wang, Y., and Weiss, A.S.: Electrospun synthetic human elastin:collagen composite scaffolds for dermal tissue engineering. Acta Biomater. 8, 3714–3722 (2012).CrossRefGoogle ScholarPubMed
Chaudhari, A., Vig, K., Baganizi, D., Sahu, R., Dixit, S., Dennis, V., Singh, S., and Pillai, S.: Future prospects for scaffolding methods and biomaterials in skin tissue engineering: A review. Int. J. Mol. Sci. 17, 1974 (2016).CrossRefGoogle ScholarPubMed
Chua, A.W.C., Khoo, Y.C., Tan, B.K., Tan, K.C., Foo, C.L., and Chong, S.J.: Skin tissue engineering advances in severe burns: Review and therapeutic applications. Burns Trauma. 4, 3 (2016).CrossRefGoogle ScholarPubMed
Ho, J., Walsh, C., Yue, D., Dardik, A., and Cheema, U.: Current advancements and strategies in tissue engineering for wound healing: A comprehensive review. Adv. Wound Care 6, 191–209 (2017).Google Scholar
Sekuła, M. and Zuba-Surma, E.K.: Biomaterials and stem cells: Promising tools in tissue engineering and biomedical applications. In Biomaterials in Regenerative Medicine (InTech, 2018); p. 361.Google Scholar
Lin, Y.K. and Liu, D.C.: Effects of pepsin digestion at different temperatures and times on properties of telopeptide-poor collagen from bird feet. Food Chem. 94, 621–625 (2006).CrossRefGoogle Scholar
Muyonga, J.H., Cole, C.G.B., and Duodu, K.G.: Fourier transform infrared (FTIR) spectroscopic study of acid soluble collagen and gelatin from skins and bones of young and adult Nile perch (Lates niloticus). Food Chem. 86, 325–332 (2004).CrossRefGoogle Scholar
Pati, F., Adhikari, B., and Dhara, S.: Isolation and characterization of fish scale collagen of higher thermal stability. Bioresour. Technol. 101, 3737–3742 (2010).CrossRefGoogle ScholarPubMed
Singh, P., Benjakul, S., Maqsood, S., and Kishimura, H.: Isolation and characterisation of collagen extracted from the skin of striped catfish (Pangasianodon hypophthalmus). Food Chem. 124, 97–105 (2011).CrossRefGoogle Scholar
Woo, J-W., Yu, S-J., Cho, S-M., Lee, Y-B., and Kim, S-B.: Extraction optimization and properties of collagen from yellowfin tuna (Thunnus albacares) dorsal skin. Food Hydrocolloids 22, 879–887 (2008).CrossRefGoogle Scholar
Doyle, B.B., Bendit, E.G., and Blout, E.R.: Infrared spectroscopy of collagen and collagen-like polypeptides. Biopolymers 14, 937–957 (1975).CrossRefGoogle ScholarPubMed
Payne, K.J. and Veis, A.: Fourier transform ir spectroscopy of collagen and gelatin solutions: Deconvolution of the amide I band for conformational studies. Biopolymers 27, 1749–1760 (1988).CrossRefGoogle ScholarPubMed
Surewicz, W.K. and Mantsch, H.H.: New insight into protein secondary structure from resolution-enhanced infrared spectra. Biochim. Biophys. Acta Protein Struct. Mol. Enzymol. 952, 115–130 (1988).CrossRefGoogle ScholarPubMed
Plepis, A.M.D.G., Goissis, G., and Das-Gupta, D.K.: Dielectric and pyroelectric characterization of anionic and native collagen. Polym. Eng. Sci. 36, 2932–2938 (1996).CrossRefGoogle Scholar
Mina, Y., MohammadReza, K., Ruhollah Mehdinavaz, A., Keyvan, S., and Masoud, R.: Optimization of electrospinning process of poly(vinyl alcohol) via response surface methodology (RSM) based on the central composite design. Curr. Chem. Lett. 3, 175–182 (2014).Google Scholar
Ortega-Arroyo, L., Martin-Martinez, E.S., Aguilar-Mendez, M.A., Cruz-Orea, A., Hernandez-Pérez, I., and Glorieux, C.: Green synthesis method of silver nanoparticles using starch as capping agent applied the methodology of surface response. Starch-Stärke. 65, 814–821 (2013).CrossRefGoogle Scholar
Bosman, F.T. and Stamenkovic, I.: Functional structure and composition of the extracellular matrix. J. Pathol. 200, 423–428 (2003).CrossRefGoogle ScholarPubMed
Lee, S.J., Yoo, J.J., Lim, G.J., Atala, A., and Stitzel, J.: In vitro evaluation of electrospun nanofiber scaffolds for vascular graft application. J. Biomed. Mater. Res., Part A 83, 999–1008 (2007).CrossRefGoogle ScholarPubMed
Su Rho, K., Jeong, L., Lee, G., Seo, B-M., Jeong Park, Y., Hong, S-D., Roh, S., Jin Cho, J., Park, W.H., and Min, B-M.: Electrospinning of collagen nanofibers: Effects on the behavior of normal human keratinocytes and early-stage wound healing. Biomaterials 27, 1452–1461 (2006).Google Scholar
Gough, J.E., Scotchford, C.A., and Downes, S.: Cytotoxicity of glutaraldehyde crosslinked collagen/poly(vinyl alcohol) films is by the mechanism of apoptosis. J. Biomed. Mater. Res. 61, 121–130 (2002).CrossRefGoogle Scholar
Jocic, S., Mestres, G., and Tenje, M.: Fabrication of user-friendly and biomimetic 1,1′-carbonyldiimidazole cross-linked gelatin/agar microfluidic devices. Mater. Sci. Eng., C 76, 1175–1180 (2017).CrossRefGoogle ScholarPubMed
Koch, H., Hammer, N., Ossmann, S., Schierle, K., Sack, U., Hofmann, J., Wecks, M., and Boldt, A.: Tissue engineering of ureteral grafts: Preparation of biocompatible crosslinked ureteral scaffolds of porcine origin. Front. Bioeng. Biotechnol. 3, 1–16 (2015).CrossRefGoogle ScholarPubMed
Haugh, M.G., Murphy, C.M., McKiernan, R.C., Altenbuchner, C., and O’Brien, F.J.: Crosslinking and mechanical properties significantly influence cell attachment, proliferation, and migration within collagen glycosaminoglycan scaffolds. Tissue Eng., Part A 17, 1201–1208 (2011).CrossRefGoogle ScholarPubMed
Powell, H.M. and Boyce, S.T.: EDC cross-linking improves skin substitute strength and stability. Biomaterials 27, 5821–5827 (2006).CrossRefGoogle ScholarPubMed
Shan, Y-H., Peng, L-H., Liu, X., Chen, X., Xiong, J., and Gao, J-Q.: Silk fibroin/gelatin electrospun nanofibrous dressing functionalized with astragaloside IV induces healing and anti-scar effects on burn wound. Int. J. Pharm. 479, 291–301 (2015).CrossRefGoogle ScholarPubMed
Zeybek, B., Duman, M., and Ürkmez, A.S.: Electrospinning of nanofibrous polycaprolactone (PCL) and collagen-blended polycaprolactone for wound dressing and tissue engineering. Usak Univ. J. Mater. Sci. 3, 121 (2014).Google Scholar
Li, M., Mondrinos, M.J., Chen, X., Gandhi, M.R., Ko, F.K., and Lelkes, P.I.: Co-electrospun poly(lactide-co-glycolide), gelatin, and elastin blends for tissue engineering scaffolds. J. Biomed. Mater. Res., Part A 79, 963–973 (2006).CrossRefGoogle Scholar