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2022 Vol.32, Issue 4 Preview Page
Cross-Linked Collagen Scaffold from Fish Skin as an Ideal Biopolymer for Tissue Engineering
Esmaeil Biazar1†
,
Mahshad Kamalvand1
,
Saeed Heidari Keshel2
,
Bahareh Pourjabbar2
,
Rezaei-Tavirani Mustafa3
1Tissue Engineering Group, Department of Biomedical Engineering, Tonekabon Branch, Islamic Azad University, Tonekabon, Iran
2Department of Tissue Engineering and Applied Cell Sciences, School of Advanced Technologies in Medicine, Shahid Beheshti University of Medical Sciences, Tehran, Iran
3Proteomics Research Center, Shahid Beheshti University of Medical Sciences, Tehran, Iran.
†Corresponding author E-Mail : kia_esm@yahoo.com (E. Biazar, Islamic Azad Univ.)
April 2022. pp. 186-192
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Abstract

Collagen is one of the most widely used biological materials in medical design. Collagen extracted from marine organisms can be a good biomaterial for tissue engineering applications due to its suitable properties. In this study, collagen is extracted from fish skin of Ctenopharyngodon Idella; then, the freeze drying method is used to design a porous scaffold. The scaffolds are modified with the chemical crosslinker N-(3-Dimethylaminopropyl)-N'-ethyl carbodiimide hydrochloride (EDC) to improve some of the overall properties. The extracted collagen samples are evaluated by various analyzes including cytotoxicity test, SDS-PAGE, FTIR, DSC, SEM, biodegradability and cell culture. The results of the SDS-PAGE study demonstrate well the protein patterns of the extracted collagen. The results show that cross-linking of collagen scaffold increases denaturation temperature and degradation time. The results of cytotoxicity show that the modified scaffolds have no toxicity. The cell adhesion study also shows that epithelial cells adhere well to the scaffold. Therefore, this method of chemical modification of collagen scaffold can improve the physical and biological properties. Overall, the modified collagen scaffold can be a promising candidate for tissue engineering applications.

Keywords
fish skin
collagen
scaffold
cross linking
physical and biological studies
References
1.
E. A. A. Neel, L. Bozec, J. C. Knowles, O. Syed, V. Mudera, R. Day and J. K. Hyun, Adv. Drug Delivery Rev., 65, 429 (2013). 10.1016/j.addr.2012.08.01022960357
2.
A. Bailey, S. Robins and G. Balian, Nature, 251, 105 (1974). 10.1038/251105a04422783
3.
J. S. Lee, J. K. Kim, Y. H. Chang and S. R. Park, Macromol. Res., 15, 205 (2007). 10.1007/BF03218776
4.
Y. Jie, Z. Cai, S. Li, Z. Xie, M. Ma and X. Huang, Macromol. Res., 25, 905 (2017). 10.1007/s13233-017-5091-z
5.
J. E. Song, N. Tripathy, J. H. Shin, D. H. Lee, J. G. Cha and C. H. Park, Macromol. Res., 25, 994 (2017). 10.1007/s13233-017-5134-5
6.
J. E. Song, N. Tripathy, J. H. Shin, D. H. Lee, C. H. Park and G. Khang, Macromol. Res., 24, 359 (2016). 10.1007/s13233-016-4051-3
7.
Z. Zhai, H. Wang, B. Wei, P. Yu, C. Xu and L. He, Macromol. Res., 26, 609 (2018). 10.1007/s13233-018-6081-5
8.
L. He, W. Lan, Y. Wang, S. Ahmed and Y. Liu, Foods, 8, 396 (2019). 10.3390/foods809039631500209PMC6769988
9.
L. A. Tziveleka, E. Ioannou, D. Tsiourvas, P. Berillis, E. Foufa and V. Roussis, Mar. Drugs, 15, 152 (2017). 10.3390/md1506015228555046PMC5484102
10.
T. Purohit, T. He, Z. Qin, T. Li, G. J. Fisher and Y. Yan, J. Dermatol. Sci., 83, 80 (2016). 10.1016/j.jdermsci.2016.04.00427132061
11.
Y. S. Lim, Y. J. Ok, S. Y. Hwang, J. Y. Kwak and S. Yoon, Mar. Drugs, 17, 467 (2019). 10.3390/md1708046731405173PMC6723527
12.
S. Shin, M. Ikram, F. Subhan, H. Y. Kang, Y. Lim and R. Lee, RSC Adv., 6, 46952 (2016). 10.1039/C6RA01937D
13.
S. K. Ghosh and D. Mandal, Appl. Phys. Lett., 109, 103701 (2016). 10.1063/1.4961623
14.
P. Vares, M. M. Dehghan, F. Bastami, E. Biazar, N. Shamloo and S. H. Keshel and A. Khojasteh, J. Craniofac. Surg., 32, 794 (2020). 10.1097/SCS.000000000000700333705038
15.
S. Akhshabi, E. Biazar, V. Singh, S. H. Keshel and N. Geetha, Int. J. Nanomedicine, 13, 4405 (2018). 10.2147/IJN.S16573930104874PMC6071624
16.
S. Heidari-Keshel, M. Ahmadian, E. Biazar, A. Gazmeh, M. Rabiei and M. Adibi, Mater. Tech., 31, 799 (2016). 10.1080/10667857.2016.1258517
17.
S. Akhshabi, E. Biazar, V. Singh, S. H. Keshel, S. Heidari-Keshel and G. Nagaraja, Mater. Tech., 33, 253 (2018). 10.1080/10667857.2017.1410998
18.
J. Ai, K. S. Heidari, F. Ghorbani, F. Ejazi, E. Biazar and A. Asefnejad, J. Nanomaterials, 2011, 123724 (2011).
19.
S. H. Keshel, E. Biazar, M. R. Tavirani, M. R. Roodsari, A. Ronaghi and M. Ebrahimi, Artif. Cells. Nanomed. Biotechnol., 42, 210 (2013). 10.3109/21691401.2013.80008023909504
20.
E. Biazar, S. H. Keshel and M. Pouya, Neural Regen. Res., 8, 2501 (2013).
21.
Y. Liu, D. Ma, Y. Wang and W. Qin, Int. J. Biol. Macromol., 106, 516 (2018). 10.1016/j.ijbiomac.2017.08.04428801096
22.
J. Hu, T. Li, X. Liu and D. Liu, Food Biosci., 15, 27 (2016). 10.1016/j.fbio.2016.04.006
23.
M. V. Bhuimbar, P. K. Bhagwat and P. B. Dandge, J. Environ. Chem. Eng., 7, 102983 (2019). 10.1016/j.jece.2019.102983
24.
W. Jimin, Y. Ping and G. Jing, Acad. Military Med. Sci., 22, 281 (1998).
25.
B. Pourjabbar, L. Hassani and H. R. Sajedi, Protein Pept. Lett., 22, 1089 (2015). 10.2174/092986652266615092910352026416699
26.
L. Tang, S. Chen, W. Su, W. Weng, K. Osako and M. Tanaka, Process Biochem., 50, 148 (2015). 10.1016/j.procbio.2014.10.015
27.
M. Koulikovska, M. Rafat, G. Petrovski, Z. Veréb, S. Akhtar and P. Fagerholm, Tissue Eng., 21, 1116 (2015). 10.1089/ten.tea.2014.056225412075
28.
Y. Jia, H. Wang, H. Wang, Y. Li, M. Wang and J. Zhou, Food Sci. Biotechnol., 21, 1585 (2012). 10.1007/s10068-012-0211-1
29.
M. Kamalvand, E. Biazar, M. Daliri-Joupari, F. Montazer, M. Rezaei-Tavirani and S. Heidari-Keshel, Tissue Cell, 71, 101509 (2021). 10.1016/j.tice.2021.10150933621947
30.
C. S. Lau, A. Hassanbhai, F. Wen, D. Wang, N. Chanchareonsook and B. T. Goh, J. Tissue Eng. Regener. Med., 13, 1779 (2019). 10.1002/term.292831278852
31.
Y. Chen, R. Ye and Y. Wang, Int. J. Food Sci. Technol., 50, 186 (2015). 10.1111/ijfs.12675
32.
M. Yan, B. Li, X. Zhao, G. Ren, Y. Zhuang and H. Hou, Food Chem., 107, 1581 (2008). 10.1016/j.foodchem.2007.10.027
33.
D. Liu, P. Zhou, T. Li and J. M. Regenstein, Food Hydrocolloids, 41, 290 (2014). 10.1016/j.foodhyd.2014.04.030
34.
J. Chen, L. Li, R. Yi, N. Xu, R. Gao and B. Hong, LWTFood Sci. Technol., 66, 453 (2016). 10.1016/j.lwt.2015.10.070
35.
P. Kittiphattanabawon, S. Nalinanon, S. Benjakul and H. Kishimura, J. Chem., 2015, 1 (2015). 10.1155/2015/482354
36.
S. Krimm and J. Bandekar, Adv. Protein Chem., 38, 181 (1986). 10.1016/S0065-3233(08)60528-8
37.
Q. Li, L. Mu, F. Zhang, Y. Sun, Q. Chen and C. Xie, Mater. Sci. Eng. C, 80, 346 (2017). 10.1016/j.msec.2017.05.10228866173
38.
M. Griffith, R. Osborne, R. Munger, X. Xiong, C. J. Doillon and N. L. Laycock, Science, 286, 2169 (1999). 10.1126/science.286.5447.216910591651
39.
S. Shimmura, C. J. Doillon, M. Griffith, M. Nakamura, E. Gagnon and A. Usui, Cornea, 22, S81 (2003). 10.1097/00003226-200310001-0001214703712
40.
C. K. Bektas and V. Hasirci, J. Tissue Eng. Regener. Med., 12, e1899 (2018). 10.1002/term.262129193831
Information
  • Publisher :Materials Research Society of Korea
  • Publisher(Ko) :한국재료학회
  • Journal Title :Korean Journal of Materials Research
  • Journal Title(Ko) :한국재료학회지
  • Volume : 32
  • No :4
  • Pages :186-192
  • Received Date : 2021-09-27
  • Revised Date : 2022-03-16
  • Accepted Date : 2022-03-22
  • DOI :https://doi.org/10.3740/MRSK.2022.32.4.186
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