화학공학소재연구정보센터
Macromolecular Research, Vol.23, No.9, 861-866, September, 2015
Characteristics of carboxymethyl cellulose/sericin hydrogels and the influence of molecular weight of carboxymethyl cellulose
E-mail:
Carboxymethyl cellulose (CMC),which is a hydrophilic polysaccharide obtained from the carboxymethylation of natural cellulose, has been formulated as hydrogel for various biomedical applications. However, the functional crosslinking agents were required to form the stable CMC hydrogels. In this study, sericin which is a glue-like protein that envelops the fibroin fiber in the silkworm cocoons was introduced to blend with CMC to form a mechanically stable hydrogel without further crosslinking. Furthermore, the effect of molecular weight of CMC on characteristics of the CMC/sericin hydrogels obtained was investigated. We found that the incorporation of sericin in CMC hydrogels enhanced the stability and the hydrogel’s resistance to hydrolysis and enzymatic degradation while the porous structure and swelling abilities of the CMC hydrogels were preserved. The in vitro biodegradation of the CMC/sericin hydrogels and the release of sericin from the hydrogels were evaluated. The biodegradability of the CMC/sericin hydrogels depended on the molecular weight of CMC. The high molecular weight CMC/sericin hydrogels showed the slowest rate of degradation. The slow-degrading high molecular weight CMC/sericin hydrogels resulted in the lowest amount of sericin release while the fast-degrading low and medium molecular weight CMC/sericin hydrogels released high amount of sericin. The high amount of sericin released from the fast-degrading low and medium molecular weight CMC/sericin hydrogels could consequently promote the collagen production of L929 cells. These CMC/sericin hydrogels could be further investigating to be applied as a wound dressing material.
  1. Gilbert RD, Cellulosic Polymers, Blends, and Composites, Hanser/Gardner Publications, Cincinnati, 1994.
  2. Wade A, Weller PJ, Handbook of Pharmaceutical Excipients, Pharmaceutical Society of Great Britain, London, 1994.
  3. Sannino A, Demitri C, Madaghiele M, Materials (Basel), 2, 353 (2009)
  4. Pasqui D, Torricelli P, Cagna MD, Fini M, Barbucci R, J. Biomed. Mater. Res. A, 102A, 1568 (2014)
  5. Bajpai AK, Giri A, Carbohydr. Polym., 53, 271 (2003)
  6. Nerurkar NL, Elliott DM, Mauck RL, J. Biomech. Eng. -Trans. ASME, 43, 1017 (2010)
  7. Kono H, Carbohydr. Polym., 106, 84 (2014)
  8. Colombo P, Bettini R, Sabti P, Peppas NA, Pharm. Sci. Technol. Today, 3, 198 (2000)
  9. Kono H, Onishi K, Nakamura T, Carbohydr. Polym., 98, 784 (2013)
  10. Akar E, Antinis KA, Seki Y, Carbohydr. Polym., 90, 1634 (2012)
  11. Song SH, Yun YP, Kim HJ, Park K, Kim SE, Song HR, Biomed Res. Int., Article ID 230152 (2014).
  12. Reeves R, Ribeiro A, Lombardo L, Boyer R, Leach JB, Polymer, 2, 252 (2010)
  13. Fana L, Peng M, Zhou X, Wu H, Hu J, Xie W, Liu S, Carbohydr. Polym., 112, 32 (2014)
  14. Zhang YQ, Biotechnol. Adv., 20, 91 (2002)
  15. Dash BC, Mandal BB, Kundu SC, J. Biotechnol., 144, 321 (2009)
  16. Zhaorigetu S, Sasaki M, Kato N, J. Nutr. Sci. Vitaminol., 53, 297 (2007)
  17. Nagai N, Murao T, Ito Y, Okamoto N, Sasaki M, Biol. Pharm. Bull., 32, 933 (2009)
  18. Aramwit P, Kanokpanont S, De-Eknamkul W, Srichana T, J. Biosci. Bioeng., 107(5), 556 (2009)
  19. Hasatsri S, Yamdech R, Chanvorachote P, Aramwit P, J. Biomater. Appl., 29, 1304 (2015)
  20. Terada S, Nishimura T, Sasaki M, Yamada H, Miki M, Cytotechnology, 40, 3 (2002)
  21. Siritientong T, Ratanavaraporn J, Srichana T, Aramwit P, Biomed Res. Int., Article ID 904314 (2013).
  22. Aramwit P, Siritienthong T, Srichana T, Ratanavaraporn J, Cells Tissues Organs, 197, 224 (2013)
  23. Siritienthong T, Ratanavaraporn J, Aramwit P, Int. J. Pharm., 439, 175 (2012)
  24. Aramwit P, Ratanavaraporn J, Ekgasit S, Tongsakul D, Bang N, J. Biomed. Mater. Res. Part B: Appl. Biomater., 103, 915 (2015)
  25. Siritientong T, Angspatt A, Ratanavaraporn J, Aramwit O, Pharm. Res., 31, 104 (2014)
  26. Aramwit P, Kanokpanont S, Nakpheng T, Srichana T, Int. J. Mol. Sci., 11(5), 2200 (2010)
  27. Shambe T, Ejembi O, Enzyme Microb. Technol., 9, 308 (1987)
  28. Mosmann T, J. Immunol. Methods, 65, 55 (1983)
  29. DeFlores LP, Ganim Z, Nicodemus RA, Tokmakoff A, J. Am. Chem. Soc., 131(9), 3385 (2009)
  30. Raso SW, Clark PL, Haase-Pettingell C, King J, Thomas GJ, J. Mol. Biol., 307, 899 (2001)
  31. Tangsadthakun C, Kanokpanont S, Sanchavanakit N, Pichyangkura R, Banaprasert T, Tabata Y, Damrongsakkul S, J. Biomater. Sci.-Polym. Ed., 18, 147 (2007)