메뉴 건너뛰기




Volumn 407, Issue 1-2, 2011, Pages 44-52

Sustained-release of protein from biodegradable sericin film, gel and sponge

Author keywords

Biodegradable; Film; Gel; Sericin; Sponge; Sustained release

Indexed keywords

ALBUMIN; FLUORESCEIN ISOTHIOCYANATE; SERICIN;

EID: 79952315804     PISSN: 03785173     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijpharm.2011.01.006     Document Type: Article
Times cited : (68)

References (49)
  • 1
    • 36148969712 scopus 로고    scopus 로고
    • The effects of sericin cream on wound hearing in rats
    • Aramwit, P., Sangcakul, A., 2007. The effects of sericin cream on wound hearing in rats. Biosci. Biotechnol. Biochem. 71, 70243-70245.
    • (2007) Biosci. Biotechnol. Biochem. , vol.71 , pp. 70243-70245
    • Aramwit, P.1    Sangcakul, A.2
  • 2
    • 77958179941 scopus 로고    scopus 로고
    • Formulation and characterization of silk sericin-PVA scaffold crosslinked with genipin
    • Aramwit, P., Siritientong, T., Kanokpanont, S., Srichana, T., 2010. Formulation and characterization of silk sericin-PVA scaffold crosslinked with genipin. Int. J. Biol. Macromol. 47, 668-675.
    • (2010) Int. J. Biol. Macromol. , vol.47 , pp. 668-675
    • Aramwit, P.1    Siritientong, T.2    Kanokpanont, S.3    Srichana, T.4
  • 3
    • 75149149000 scopus 로고    scopus 로고
    • Chitosan-based hydrogels for controlled, localized drug delivery
    • Bhattarai, N., Gunn, J., Zhang, M., 2010. Chitosan-based hydrogels for controlled, localized drug delivery. Adv. Drug Deliv. Rev. 62, 83-99.
    • (2010) Adv. Drug Deliv. Rev. , vol.62 , pp. 83-99
    • Bhattarai, N.1    Gunn, J.2    Zhang, M.3
  • 4
    • 55649119573 scopus 로고    scopus 로고
    • Treatment of silk production wastewaters by membrane processes for sericin recovery
    • Capar, G., Aygun, S.S., Gecit, M.R., 2008. Treatment of silk production wastewaters by membrane processes for sericin recovery. J. Membr. Sci. 325, 920-931.
    • (2008) J. Membr. Sci. , vol.325 , pp. 920-931
    • Capar, G.1    Aygun, S.S.2    Gecit, M.R.3
  • 5
    • 70449722767 scopus 로고    scopus 로고
    • Silk gland sericin protein membrane: Fabrication and characterization for potential biotechnological applications
    • Dash, B.C., Biman, B., Kundu, S.C., 2009. Silk gland sericin protein membrane: fabrication and characterization for potential biotechnological applications. J. Biotechnol. 144, 321-329.
    • (2009) J. Biotechnol. , vol.144 , pp. 321-329
    • Dash, B.C.1    Biman, B.2    Kundu, S.C.3
  • 6
    • 41349084565 scopus 로고    scopus 로고
    • Silk sericin protein of tropical tasar silkworm inhibits UVB-induced apoptosis in human skin keratinocytes
    • Dash, R., Mandal, M., Ghosh, S.K., Kundu, S.C., 2008a. Silk sericin protein of tropical tasar silkworm inhibits UVB-induced apoptosis in human skin keratinocytes. Mol. Cell Biochem. 311, 111-119.
    • (2008) Mol. Cell Biochem. , vol.311 , pp. 111-119
    • Dash, R.1    Mandal, M.2    Ghosh, S.K.3    Kundu, S.C.4
  • 7
    • 42049106232 scopus 로고    scopus 로고
    • Antioxidant potential of silk protein sericin against hydrogen peroxide-induced oxidative stress in skin fibroblasts
    • Dash, R., Acharya, C., Bindu, P., Kundu, S.C., 2008b. Antioxidant potential of silk protein sericin against hydrogen peroxide-induced oxidative stress in skin fibroblasts. BMB Rep. 41, 236-241. (Pubitemid 351518997)
    • (2008) Journal of Biochemistry and Molecular Biology , vol.41 , Issue.3 , pp. 236-241
    • Dash, R.1    Acharya, C.2    Bindu, P.C.3    Kundu, S.C.4
  • 8
    • 0242578416 scopus 로고    scopus 로고
    • Degumming of silk fabric with several proteases
    • DOI 10.1016/j.jbiotec.2003.09.006
    • Freddi, G., Mossotti, R., Innocenti, R., 2003. Degumming of silk fabric with several proteases. J. Biotechnol. 106, 101-112. (Pubitemid 37421377)
    • (2003) Journal of Biotechnology , vol.106 , Issue.1 , pp. 101-112
    • Freddi, G.1    Mossotti, R.2    Innocenti, R.3
  • 9
    • 0020038059 scopus 로고
    • Genetic variants of the Bombyx mori silkworm encoding sericin proteins of different lengths
    • Gamo, T., 1982. Genetic variants of the Bombyx mori silkworm encoding sericin proteins of different lengths. Biochem. Genet. 20, 165-177.
    • (1982) Biochem. Genet. , vol.20 , pp. 165-177
    • Gamo, T.1
  • 10
    • 0031148815 scopus 로고    scopus 로고
    • Structure and organization of the Bombyx mori Sericin 1 gene and of the Sericins 1 deduced from the sequence of the Ser 1B cDNA
    • Garel, A., Deleage, G., Prudhomme, J.-C., 1997. Structure and organization of the Bombyx mori Sericin 1 gene and of the Sericins 1 deduced from the sequence of the Ser 1B cDNA. Insect. Biochem. Mol. Biol. 27, 469-477.
    • (1997) Insect. Biochem. Mol. Biol. , vol.27 , pp. 469-477
    • Garel, A.1    Deleage, G.2    Prudhomme, J.-C.3
  • 11
    • 33847307132 scopus 로고    scopus 로고
    • Controlled-release of epidermal growth factor from cationized gelatin hydrogel enhances corneal epithelial wound healing
    • DOI 10.1016/j.jconrel.2006.12.011, PII S0168365906007024
    • Hori, K., Sotozono, C., Hamuro, J., Yamasaki, K., Kimura, Y., Ozeki, M., Tabata, Y., Kinoshita, S., 2007. Controlled-release of epidermal growth factor from cationized gelatin hydrogel enhances corneal epithelial wound healing. J. Control. Release 118, 169-176. (Pubitemid 46329733)
    • (2007) Journal of Controlled Release , vol.118 , Issue.2 , pp. 169-176
    • Hori, K.1    Sotozono, C.2    Hamuro, J.3    Yamasaki, K.4    Kimura, Y.5    Ozeki, M.6    Tabata, Y.7    Kinoshita, S.8
  • 12
    • 68649090915 scopus 로고    scopus 로고
    • Enhancement of gene transfection into human dendric cells using cationic PLGA nanospheres with a synthesized nuclear localization signal
    • Kanazawa, T., Takashima, Y., Murakoshi, M., Nakai, Y., Okada, H., 2009. Enhancement of gene transfection into human dendric cells using cationic PLGA nanospheres with a synthesized nuclear localization signal. Int. J. Pharm. 379, 187-195.
    • (2009) Int. J. Pharm. , vol.379 , pp. 187-195
    • Kanazawa, T.1    Takashima, Y.2    Murakoshi, M.3    Nakai, Y.4    Okada, H.5
  • 13
    • 37349035782 scopus 로고    scopus 로고
    • Effect of chitosan on the release of protein from thermosensitive poly(organophosphazene) hydrogels
    • Kang, G.D., Song, S.C., 2008. Effect of chitosan on the release of protein from thermosensitive poly(organophosphazene) hydrogels. Int. J. Pharm. 349, 188-195.
    • (2008) Int. J. Pharm. , vol.349 , pp. 188-195
    • Kang, G.D.1    Song, S.C.2
  • 15
    • 79952312983 scopus 로고    scopus 로고
    • Development of mammalian factors-free medium for cell culture by using silk protein sericin
    • Kobayashi, M., Sakuma, A., Kunitomi, Y., Sasaki, M., Yamada, H., Terada, S., 2009. Development of mammalian factors-free medium for cell culture by using silk protein sericin. J. Biosci. Bioeng. 108., S18-S19.
    • (2009) J. Biosci. Bioeng. , vol.108
    • Kobayashi, M.1    Sakuma, A.2    Kunitomi, Y.3    Sasaki, M.4    Yamada, H.5    Terada, S.6
  • 16
    • 84991136795 scopus 로고
    • Chemical studies on sericin. II. Amino acid composition of wilds and domestic cocoon sericin
    • Komatsu, K., Yamada, M., 1975. Chemical studies on sericin. II. Amino acid composition of wilds and domestic cocoon sericin. J. Seric. Sci. Jpn. 44, 105-110.
    • (1975) J. Seric. Sci. Jpn. , vol.44 , pp. 105-110
    • Komatsu, K.1    Yamada, M.2
  • 17
    • 0009848063 scopus 로고
    • Studies on dissolution behavior and structural characteristics of silk sericin
    • Agriculture, Forestry and Fisheries Research Council Secretariat, Tukuba
    • Komatsu, K., 1975. Studies on dissolution behavior and structural characteristics of silk sericin, Sanshi-shikenjo-houkoku, Vol. 26. Agriculture, Forestry and Fisheries Research Council Secretariat, Tukuba, pp. 135-256.
    • (1975) Sanshi-shikenjo-houkoku , vol.26 , pp. 135-256
    • Komatsu, K.1
  • 18
    • 55649095103 scopus 로고    scopus 로고
    • Natural protective glue protein, sericin bioengineered by silkworms: Potential for biomedical and biotechnological applications
    • Kundu, S.C., Dash, B.C., Dash, R., Kaplanm, D.L., 2008. Natural protective glue protein, sericin bioengineered by silkworms: potential for biomedical and biotechnological applications. Prog. Polym. Sci. 33, 998-1012.
    • (2008) Prog. Polym. Sci. , vol.33 , pp. 998-1012
    • Kundu, S.C.1    Dash, B.C.2    Dash, R.3    Kaplanm, D.L.4
  • 19
    • 33745634172 scopus 로고    scopus 로고
    • Controlled release of plasmid DNA from hydrogels prepared from gelatin cationized by different amine compounds
    • DOI 10.1016/j.jconrel.2006.02.003, PII S0168365906000721
    • Kushibiki, T., Tomoshige, R., Iwanaga, K., Kakemi, M., Tabata, Y., 2006. Controlled release of plasmid DNA from hydrogels prepared from gelatin cationized by different amine compounds. J. Control. Release 112, 249-256. (Pubitemid 44304349)
    • (2006) Journal of Controlled Release , vol.112 , Issue.2 , pp. 249-256
    • Kushibiki, T.1    Tomoshige, R.2    Iwanaga, K.3    Kakemi, M.4    Tabata, Y.5
  • 20
    • 0021917947 scopus 로고
    • Preparation and in vitro degradation properties of polylactide microcapsules
    • Makino, K., Arakawa, M., Kondo, T., 1985. Preparation and in vitro degradation properties of polylactide microcapsules. Chem. Pharm. Bull. 33, 1195-1201.
    • (1985) Chem. Pharm. Bull. , vol.33 , pp. 1195-1201
    • Makino, K.1    Arakawa, M.2    Kondo, T.3
  • 21
    • 70249135750 scopus 로고    scopus 로고
    • Novel silk sericin/gelatin 3-D scaffolds and 2-D films: Fabrication and characterization for potential tissue engineering applications
    • Mandal, B.B., Priya, A.S., Kundu, S.C., 2009. Novel silk sericin/gelatin 3-D scaffolds and 2-D films: fabrication and characterization for potential tissue engineering applications. Acta Biomater. 5, 3007-3020.
    • (2009) Acta Biomater. , vol.5 , pp. 3007-3020
    • Mandal, B.B.1    Priya, A.S.2    Kundu, S.C.3
  • 22
    • 33748519862 scopus 로고    scopus 로고
    • A new silkworm race for sericin production, "Sericin Hope" and its product "Virgin Sericin"
    • Mase, K., Iizuka, T., Okada, E., Miyajima, T., Yamamoto, T., 2006. A new silkworm race for sericin production, "Sericin Hope" and its product "Virgin Sericin". J. Insect. Biotechnol. Sericol. 75, 85-88.
    • (2006) J. Insect. Biotechnol. Sericol. , vol.75 , pp. 85-88
    • Mase, K.1    Iizuka, T.2    Okada, E.3    Miyajima, T.4    Yamamoto, T.5
  • 23
    • 0025265639 scopus 로고
    • Cloning and characterization of the highly polymorphic Ser2 gene of Bombyx mori
    • DOI 10.1016/0378-1119(90)90277-X
    • Michaille, J.-J, Garel, A., Prudhomme, J.-C., 1990. Cloning and characterization of the highly polymorphic Ser 2 gene of Bombyx mori. Gene 86, 177-184. (Pubitemid 20098903)
    • (1990) Gene , vol.86 , Issue.2 , pp. 177-184
    • Michaille, J.-J.1    Garel, A.2    Prudhomme, J.-C.3
  • 24
    • 0029380445 scopus 로고
    • Attachment and growth of cultured fibroblast cells on silk protein matrices
    • Minoura, N., Aiba, S., Gotoh, Y., Tsukada, M., Imai, T., 1995. Attachment and growth of cultured fibroblast cells on silk protein matrices. J. Biomed. Mater. Res. 29, 1215-1221.
    • (1995) J. Biomed. Mater. Res. , vol.29 , pp. 1215-1221
    • Minoura, N.1    Aiba, S.2    Gotoh, Y.3    Tsukada, M.4    Imai, T.5
  • 25
    • 79952314467 scopus 로고    scopus 로고
    • Cryopreservation of human adipose tissue-derived stem/progenitor cells using the silk protein sericin
    • Miyamoto, Y., Oishi, k., Yukawa, H., Noguchi, H., Sasaki, M., Iwata, H., Hayashi, S., 2009. Cryopreservation of human adipose tissue-derived stem/progenitor cells using the silk protein sericin. J. Cryobiol. 59, 376-377.
    • (2009) J. Cryobiol. , vol.59 , pp. 376-377
    • Miyamoto, Y.1    Oishi, K.2    Yukawa, H.3    Noguchi, H.4    Sasaki, M.5    Iwata, H.6    Hayashi, S.7
  • 26
    • 78049452879 scopus 로고    scopus 로고
    • Use of silk protein, sericin, as a sustained-release material in the form of a gel, sponge and film
    • Nishida, A., Yamada, M., Kanazawa, T., Takashima, Y., Ouchi, K., Okada, H., 2010. Use of silk protein, sericin, as a sustained-release material in the form of a gel, sponge and film. Chem. Pharm. Bull. 58, 1480-1486.
    • (2010) Chem. Pharm. Bull. , vol.58 , pp. 1480-1486
    • Nishida, A.1    Yamada, M.2    Kanazawa, T.3    Takashima, Y.4    Ouchi, K.5    Okada, H.6
  • 27
    • 33846391305 scopus 로고    scopus 로고
    • Generation of a transgenic silkworm that secretes recombinant proteins in the sericin layer of cocoon: Production of recombinant human serum albumin
    • DOI 10.1016/j.jbiotec.2006.10.019, PII S0168165606009692
    • Ogawa, S., Tomita, M., Shimizu, K., Yoshizato, K., 2007. Generation of a transgenic silkworm that secretes recombinant proteins in the sericin layer of cocoon: production of recombinant human serum albumin. J. Biotechnol. 128, 531-544. (Pubitemid 46135790)
    • (2007) Journal of Biotechnology , vol.128 , Issue.3 , pp. 531-544
    • Ogawa, S.1    Tomita, M.2    Shimizu, K.3    Yoshizato, K.4
  • 28
    • 0028029215 scopus 로고
    • Preparation of three-month depot injectable microspheres of leuprorelin acetate using biodegradable polymers
    • Okada, H., Doken, Y., Ogawa, Y., Toguchi, H., 1994. Preparation of three-month depot injectable microspheres of leuprorelin acetate using biodegradable polymers. Pharm. Res. 11, 1143-1147.
    • (1994) Pharm. Res. , vol.11 , pp. 1143-1147
    • Okada, H.1    Doken, Y.2    Ogawa, Y.3    Toguchi, H.4
  • 30
    • 0020407605 scopus 로고
    • Structural analysis of sericin gene
    • Okamoto, H., Ishikawa, E., Suzuki, Y., 1982. Structural analysis of sericin gene. J. Biol. Chem. 257, 15192-15199.
    • (1982) J. Biol. Chem. , vol.257 , pp. 15192-15199
    • Okamoto, H.1    Ishikawa, E.2    Suzuki, Y.3
  • 31
    • 0032879676 scopus 로고    scopus 로고
    • Vascularization effect of basic fibroblast growth factor released from gelatin hydrogels with different biodegradabilities
    • DOI 10.1016/S0142-9612(99)00121-0, PII S0142961299001210
    • Tabata, Y., Ikada, Y., 1999. Vascularization effect of basic fibroblast growth factor released from gelatin hydrogels with different biodegradabilities. Biomaterials 20, 2169-2175. (Pubitemid 29488666)
    • (1999) Biomaterials , vol.20 , Issue.22 , pp. 2169-2175
    • Tabata, Y.1    Ikada, Y.2
  • 32
    • 0033010667 scopus 로고    scopus 로고
    • Biodegradation of hydrogel carrier incorporating fibroblast growth factor
    • Tabata, Y., Nagano, A., Ikada, Y., 1999. Biodegradation of hydrogel carrier Incorporating fibroblast growth factor. Tissue Eng. 5, 127-138. (Pubitemid 29196555)
    • (1999) Tissue Engineering , vol.5 , Issue.2 , pp. 127-138
    • Tabata, Y.1    Nagano, A.2    Ikada, Y.3    Ikada, Y.4
  • 34
    • 0043204291 scopus 로고    scopus 로고
    • Isolation of three main sericin components from the cocoon of the silk worm, Bombyx mori
    • Takasu, Y., Yamada, H., Tsubouchi, K., 2002. Isolation of three main sericin components from the cocoon of the silk worm, Bombyx mori. Biosci. Biotechnol. Biochem. 66, 2715-2718.
    • (2002) Biosci. Biotechnol. Biochem. , vol.66 , pp. 2715-2718
    • Takasu, Y.1    Yamada, H.2    Tsubouchi, K.3
  • 35
    • 77955549366 scopus 로고    scopus 로고
    • Tracheal defect repair using a PLGA-collagen hybrid scaffold reinforced by a copolymer stent with bFGF-impregnated gelatin hydrogel
    • Takekawa, Y., Kawazoe, N., Chen, G., Shirasaki, Y., Komuro, H., Kaneko, M., 2010. Tracheal defect repair using a PLGA-collagen hybrid scaffold reinforced by a copolymer stent with bFGF-impregnated gelatin hydrogel. Pediatr. Surg. Int. 26, 575-580.
    • (2010) Pediatr. Surg. Int. , vol.26 , pp. 575-580
    • Takekawa, Y.1    Kawazoe, N.2    Chen, G.3    Shirasaki, Y.4    Komuro, H.5    Kaneko, M.6
  • 38
    • 15944391324 scopus 로고    scopus 로고
    • Preparation and structure of porous silk sericin materials
    • Tao, W., Mingzhong, L., Xie, R., 2005. Preparation and structure of porous silk sericin materials. Macromol. Mater. Eng. 290, 188-194.
    • (2005) Macromol. Mater. Eng. , vol.290 , pp. 188-194
    • Tao, W.1    Mingzhong, L.2    Xie, R.3
  • 40
    • 22944481530 scopus 로고    scopus 로고
    • Molecular orientation behavior of silk sericin film as revealed by ATR infrared spectroscopy
    • DOI 10.1021/bm0500547
    • Teramoto, H., Miyazawa, M., 2005. Molecular orientation behavior of silk sericin film as revealed by ATR infrared spectroscopy. Biomacromolecules 6, 2049-2057. (Pubitemid 41052198)
    • (2005) Biomacromolecules , vol.6 , Issue.4 , pp. 2049-2057
    • Teramoto, H.1    Miyazawa, M.2
  • 41
    • 58149085875 scopus 로고    scopus 로고
    • Preparation of gel film from Bombyx mori silk sericin and its characterization as awound dressing
    • Teramoto, H., Kameda, T., Tamada, Y., 2008. Preparation of gel film from Bombyx mori silk sericin and its characterization as awound dressing. Biosci. Biotechnol. Biochem. 72, 3189-3196.
    • (2008) Biosci. Biotechnol. Biochem. , vol.72 , pp. 3189-3196
    • Teramoto, H.1    Kameda, T.2    Tamada, Y.3
  • 42
    • 33947270958 scopus 로고    scopus 로고
    • Native structure and degradation pattern of silk sericin studied by 13C NMR spectroscopy
    • Teramoto, H., Kakazu, A., Yamauchi, K., Asakura, T., 2007. Native structure and degradation pattern of silk sericin studied by 13C NMR spectroscopy. Macromolecules 40, 1562-1569.
    • (2007) Macromolecules , vol.40 , pp. 1562-1569
    • Teramoto, H.1    Kakazu, A.2    Yamauchi, K.3    Asakura, T.4
  • 43
    • 34447315265 scopus 로고    scopus 로고
    • A germline transgenic silkworm that secretes recombinant proteins in the sericin layer of cocoon
    • DOI 10.1007/s11248-007-9087-x
    • Tomita, M., Hino, R., Ogawa, S., Iizuka, M., Adachi, T., Shimizu, K., Sotoshiro, H., Yoshizato, K., 2007. A germline transgenic silkworm that secretes recombinant proteins in the sericin layer of cocoon. Transgenic Res. 16, 449-465. (Pubitemid 47052121)
    • (2007) Transgenic Research , vol.16 , Issue.4 , pp. 449-465
    • Tomita, M.1    Hino, R.2    Ogawa, S.3    Iizuka, M.4    Adachi, T.5    Shimizu, K.6    Sotoshiro, H.7    Yoshizato, K.8
  • 44
    • 79952317682 scopus 로고    scopus 로고
    • Japanese Patent No.11-070160A
    • Tsubouchi, K., 1999. Japanese Patent No.11-070160A.
    • (1999)
    • Tsubouchi, K.1
  • 46
    • 0001733541 scopus 로고    scopus 로고
    • Structures and physical properties of poly(vinyl alcohol)/sericin blend hydrogel membranes
    • Wang, S., Goto, Y., Ohkoshi, Y., Nagura, M., 1998. Structures and physical properties of poly(vinyl alcohol)/sericin blend hydrogel membranes. J. Seric. Sci. Jpn. 4, 295-302.
    • (1998) J. Seric. Sci. Jpn. , vol.4 , pp. 295-302
    • Wang, S.1    Goto, Y.2    Ohkoshi, Y.3    Nagura, M.4
  • 47
    • 0036268771 scopus 로고    scopus 로고
    • Applications of natural silk protein sericin in biomaterials
    • Zhang, Y.-Q., 2002. Applications of natural silk protein sericin in biomaterials. Biotechnol. Adv. 20, 91-100.
    • (2002) Biotechnol. Adv. , vol.20 , pp. 91-100
    • Zhang, Y.-Q.1
  • 48
    • 1542298821 scopus 로고    scopus 로고
    • Immobilization of L-asparaginase on the microparticles of the natural silk sericin protein and its characters
    • DOI 10.1016/j.biomaterials.2003.10.019, PII S0142961203009347
    • Zhang, Y.-Q., Tao, M.-L., Shen, W.-D., Zhou, Y.-Z., Ding, Y.-D., Ma, Y., Zhou, W.-L., 2004. Immobilization of L-asparaginase on the microparticles of the natural silk sericin protein and its characters. Biomaterials 25, 3751-3759. (Pubitemid 38327064)
    • (2004) Biomaterials , vol.25 , Issue.17 , pp. 3751-3759
    • Zhang, Y.-Q.1    Tao, M.-L.2    Shen, W.-D.3    Zhou, Y.-Z.4    Ding, Y.5    Ma, Y.6    Zhou, W.-L.7
  • 49
    • 0001370121 scopus 로고
    • Gelation of silk sericin and physical properties of the gel
    • Zhu, L.J., Arai, M., Hirabayashi, K., 1995. Gelation of silk sericin and physical properties of the gel. J. Sericult. Sci. Jpn. 64, 415-419.
    • (1995) J. Sericult. Sci. Jpn. , vol.64 , pp. 415-419
    • Zhu, L.J.1    Arai, M.2    Hirabayashi, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.