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Volumn 254, Issue , 2014, Pages 488-493

Structure and characteristics of milled silk particles

Author keywords

Bead mill; Ion adsorption; Silk nanoparticle; Silk particle characterization

Indexed keywords

AMORPHOUS CONTENT; BEAD MILLS; CHARGE REPULSION; DECOMPOSITION TEMPERATURE; INTER-MOLECULAR FORCES; ION ADSORPTION; PARTICLE CHARACTERIZATION; STERIC REPULSIONS;

EID: 84896717100     PISSN: 00325910     EISSN: 1873328X     Source Type: Journal    
DOI: 10.1016/j.powtec.2014.01.060     Document Type: Article
Times cited : (19)

References (45)
  • 3
    • 0030196210 scopus 로고    scopus 로고
    • Evidence of a cholesteric liquid crystalline phase in natural silk spinning processes
    • Willcox P.J., Gido S.P., Muller W., Kaplan D.L. Evidence of a cholesteric liquid crystalline phase in natural silk spinning processes. Macromolecules 1996, 29:5106-5110.
    • (1996) Macromolecules , vol.29 , pp. 5106-5110
    • Willcox, P.J.1    Gido, S.P.2    Muller, W.3    Kaplan, D.L.4
  • 4
    • 0033731020 scopus 로고    scopus 로고
    • Atomic force microscopy: Bombyx mori silk fibroin molecules and their higher order structure
    • Inoue S.-I., Magoshi J., Tanaka T., Magoshi Y., Becker M. Atomic force microscopy: Bombyx mori silk fibroin molecules and their higher order structure. J. Polym. Sci. B Polym. Phys. 2000, 38:1436-1439.
    • (2000) J. Polym. Sci. B Polym. Phys. , vol.38 , pp. 1436-1439
    • Inoue, S.-I.1    Magoshi, J.2    Tanaka, T.3    Magoshi, Y.4    Becker, M.5
  • 9
    • 79952987084 scopus 로고    scopus 로고
    • Silk fibroin as a vehicle for drug delivery applications
    • Wenk E., Merkle H.P., Meinel L. Silk fibroin as a vehicle for drug delivery applications. J. Control. Release 2011, 150:128-141.
    • (2011) J. Control. Release , vol.150 , pp. 128-141
    • Wenk, E.1    Merkle, H.P.2    Meinel, L.3
  • 11
    • 80054679810 scopus 로고    scopus 로고
    • Release and cellular acceptance of multiple drugs loaded silk fibroin particles
    • Shi P., Goh J.C.H. Release and cellular acceptance of multiple drugs loaded silk fibroin particles. Int. J. Pharm. 2011, 420:282-289.
    • (2011) Int. J. Pharm. , vol.420 , pp. 282-289
    • Shi, P.1    Goh, J.C.H.2
  • 14
    • 0025700773 scopus 로고    scopus 로고
    • Preparation and characterization of silk fibroin powder and its application to enzyme immobilization
    • Yoshimizu H., Asakura T. Preparation and characterization of silk fibroin powder and its application to enzyme immobilization. J. Appl. Polym. Sci. 2003, 40:127-134.
    • (2003) J. Appl. Polym. Sci. , vol.40 , pp. 127-134
    • Yoshimizu, H.1    Asakura, T.2
  • 16
    • 0030237152 scopus 로고    scopus 로고
    • Effects of non-formaldehyde finishing process on dyeing and mechanical properties of cotton fabrics
    • Kawahara Y., Shioya M., Takaku A. Effects of non-formaldehyde finishing process on dyeing and mechanical properties of cotton fabrics. Am. Dyest Rep. 1996, 85:88-91.
    • (1996) Am. Dyest Rep. , vol.85 , pp. 88-91
    • Kawahara, Y.1    Shioya, M.2    Takaku, A.3
  • 17
    • 44949167731 scopus 로고    scopus 로고
    • Silk fibroin protein from mulberry and non-mulberry silkworms: cytotoxicity, biocompatibility and kinetics of L929 murine fibroblast adhesion
    • Acharya C., Ghosh S.K., Kundu S. Silk fibroin protein from mulberry and non-mulberry silkworms: cytotoxicity, biocompatibility and kinetics of L929 murine fibroblast adhesion. J. Mater. Sci. Mater. Med. 2008, 19:2827-2836.
    • (2008) J. Mater. Sci. Mater. Med. , vol.19 , pp. 2827-2836
    • Acharya, C.1    Ghosh, S.K.2    Kundu, S.3
  • 18
    • 70350700449 scopus 로고    scopus 로고
    • Animal silks: their structures, properties and artificial production
    • Fu C., Shao Z., Fritz V. Animal silks: their structures, properties and artificial production. Chem. Commun. 2009, 6515-6529.
    • (2009) Chem. Commun. , pp. 6515-6529
    • Fu, C.1    Shao, Z.2    Fritz, V.3
  • 19
    • 77956181774 scopus 로고    scopus 로고
    • Composite materials based on silk proteins
    • Hardy J.G., Scheibel T.R. Composite materials based on silk proteins. Prog. Polym. Sci. 2010, 35:1093-1115.
    • (2010) Prog. Polym. Sci. , vol.35 , pp. 1093-1115
    • Hardy, J.G.1    Scheibel, T.R.2
  • 20
    • 84861889166 scopus 로고    scopus 로고
    • Self-assembled silk fibroin particles: tunable size and appearance
    • Shi P., Goh J.C.H. Self-assembled silk fibroin particles: tunable size and appearance. Powder Technol. 2012, 215-216:85-90.
    • (2012) Powder Technol. , pp. 85-90
    • Shi, P.1    Goh, J.C.H.2
  • 21
    • 34250620380 scopus 로고    scopus 로고
    • The preparation of regenerated silk fibroin microspheres
    • Cao Z., Chen X., Yao J., Huang L., Shao Z. The preparation of regenerated silk fibroin microspheres. Soft Matter 2007, 3:910-915.
    • (2007) Soft Matter , vol.3 , pp. 910-915
    • Cao, Z.1    Chen, X.2    Yao, J.3    Huang, L.4    Shao, Z.5
  • 24
    • 84884134908 scopus 로고    scopus 로고
    • Ultrafine silk powder from biocompatible surfactant-assisted milling
    • Kazemimostaghim M., Rajkhowa R., Tsuzuki T., Wang X. Ultrafine silk powder from biocompatible surfactant-assisted milling. Powder Technol. 2013, 249:253-257.
    • (2013) Powder Technol. , vol.249 , pp. 253-257
    • Kazemimostaghim, M.1    Rajkhowa, R.2    Tsuzuki, T.3    Wang, X.4
  • 27
    • 78249238837 scopus 로고    scopus 로고
    • Molecular weight and secondary structure change in Eri silk during alkali degumming and powdering
    • Rajkhowa R., Wang L., Kanwar J.R., Wang X. Molecular weight and secondary structure change in Eri silk during alkali degumming and powdering. J. Appl. Polym. Sci. 2011, 119:1339-1347.
    • (2011) J. Appl. Polym. Sci. , vol.119 , pp. 1339-1347
    • Rajkhowa, R.1    Wang, L.2    Kanwar, J.R.3    Wang, X.4
  • 28
    • 60449112162 scopus 로고    scopus 로고
    • Fabrication of ultrafine powder from Eri silk through attritor and jet milling
    • Rajkhowa R., Wang L., Kanwar J., Wang X. Fabrication of ultrafine powder from Eri silk through attritor and jet milling. Powder Technol. 2009, 191:155-163.
    • (2009) Powder Technol. , vol.191 , pp. 155-163
    • Rajkhowa, R.1    Wang, L.2    Kanwar, J.3    Wang, X.4
  • 29
    • 0037194006 scopus 로고    scopus 로고
    • Regenerated silk fibroin films: thermal and dynamic mechanical analysis
    • Motta A., Fambri L., Migliaresi C. Regenerated silk fibroin films: thermal and dynamic mechanical analysis. Macromol. Chem. Phys. 2002, 203:1658-1665.
    • (2002) Macromol. Chem. Phys. , vol.203 , pp. 1658-1665
    • Motta, A.1    Fambri, L.2    Migliaresi, C.3
  • 30
    • 0000951118 scopus 로고
    • Conformational characterization of Bombyx mori silk fibroin in the solid state by high-frequency carbon-13 cross polarization-magic angle spinning NMR, X-ray diffraction, and infrared spectroscopy
    • Asakura T., Kuzuhara A., Tabeta R., Saito H. Conformational characterization of Bombyx mori silk fibroin in the solid state by high-frequency carbon-13 cross polarization-magic angle spinning NMR, X-ray diffraction, and infrared spectroscopy. Macromolecules 1985, 18:1841-1845.
    • (1985) Macromolecules , vol.18 , pp. 1841-1845
    • Asakura, T.1    Kuzuhara, A.2    Tabeta, R.3    Saito, H.4
  • 31
    • 0034023387 scopus 로고    scopus 로고
    • Conformational transitions in model silk peptides
    • Wilson D., Valluzzi R., Kaplan D. Conformational transitions in model silk peptides. Biophys. J. 2000, 78:2690-2701.
    • (2000) Biophys. J. , vol.78 , pp. 2690-2701
    • Wilson, D.1    Valluzzi, R.2    Kaplan, D.3
  • 32
    • 34147152672 scopus 로고    scopus 로고
    • Protein secondary structure and orientation in silk as revealed by Raman spectromicroscopy
    • Lefèvre T., Rousseau M.-E., Pézolet M. Protein secondary structure and orientation in silk as revealed by Raman spectromicroscopy. Biophys. J. 2007, 92:2885-2895.
    • (2007) Biophys. J. , vol.92 , pp. 2885-2895
    • Lefèvre, T.1    Rousseau, M.-E.2    Pézolet, M.3
  • 33
    • 33749569009 scopus 로고    scopus 로고
    • Advances in vibrational spectroscopy as a sensitive probe of peptide and protein structure: a critical review
    • Schweitzer-Stenner R. Advances in vibrational spectroscopy as a sensitive probe of peptide and protein structure: a critical review. Vib. Spectrosc. 2006, 42:98-117.
    • (2006) Vib. Spectrosc. , vol.42 , pp. 98-117
    • Schweitzer-Stenner, R.1
  • 34
    • 0019018741 scopus 로고    scopus 로고
    • Crystallinity in silk fibers: partial acid hydrolysis and related studies
    • Bhat N., Nadiger G. Crystallinity in silk fibers: partial acid hydrolysis and related studies. J. Appl. Polym. Sci. 2003, 25:921-932.
    • (2003) J. Appl. Polym. Sci. , vol.25 , pp. 921-932
    • Bhat, N.1    Nadiger, G.2
  • 35
    • 84864988806 scopus 로고    scopus 로고
    • Structure and biodegradation mechanism of milled Bombyx mori silk particles
    • Rajkhowa R., Hu X., Tsuzuki T., Kaplan D.L., Wang X. Structure and biodegradation mechanism of milled Bombyx mori silk particles. Biomacromolecules 2012, 13:2503-2512.
    • (2012) Biomacromolecules , vol.13 , pp. 2503-2512
    • Rajkhowa, R.1    Hu, X.2    Tsuzuki, T.3    Kaplan, D.L.4    Wang, X.5
  • 36
    • 33747102801 scopus 로고    scopus 로고
    • Studies on the effects of the enzymatic treatment on silk fine powder
    • Xu W., Ke G., Peng X. Studies on the effects of the enzymatic treatment on silk fine powder. J. Appl. Polym. Sci. 2006, 101:2967-2971.
    • (2006) J. Appl. Polym. Sci. , vol.101 , pp. 2967-2971
    • Xu, W.1    Ke, G.2    Peng, X.3
  • 37
    • 0345530749 scopus 로고    scopus 로고
    • Controlling molecular conformation of regenerated wild silk fibroin by aqueous ethanol treatment
    • Li M., Tao W., Kuga S., Nishiyama Y. Controlling molecular conformation of regenerated wild silk fibroin by aqueous ethanol treatment. Polym. Adv. Technol. 2003, 14:694-698.
    • (2003) Polym. Adv. Technol. , vol.14 , pp. 694-698
    • Li, M.1    Tao, W.2    Kuga, S.3    Nishiyama, Y.4
  • 38
    • 84869222341 scopus 로고    scopus 로고
    • Chemical, structural and thermal properties of Gonometa postica silk fibroin, a potential biomaterial
    • Mhuka V., Dube S., Nindi M.M. Chemical, structural and thermal properties of Gonometa postica silk fibroin, a potential biomaterial. Int. J. Biol. Macromol. 2013, 52:305-311.
    • (2013) Int. J. Biol. Macromol. , vol.52 , pp. 305-311
    • Mhuka, V.1    Dube, S.2    Nindi, M.M.3
  • 39
    • 0342733674 scopus 로고    scopus 로고
    • Thermal behavior of regenerated Antheraea pernyi silk fibroin film treated with aqueous methanol
    • Kweon H., Um I., Park Y. Thermal behavior of regenerated Antheraea pernyi silk fibroin film treated with aqueous methanol. Polymer 2000, 41:7361-7367.
    • (2000) Polymer , vol.41 , pp. 7361-7367
    • Kweon, H.1    Um, I.2    Park, Y.3
  • 40
    • 0001520971 scopus 로고    scopus 로고
    • Structure and physical properties of silk fibroin/polyacrylamide blend films
    • Freddi G., Tsukada M., Beretta S. Structure and physical properties of silk fibroin/polyacrylamide blend films. J. Appl. Polym. Sci. 1999, 71:1563-1571.
    • (1999) J. Appl. Polym. Sci. , vol.71 , pp. 1563-1571
    • Freddi, G.1    Tsukada, M.2    Beretta, S.3
  • 41
    • 0035921099 scopus 로고    scopus 로고
    • Structural characteristics and properties of the regenerated silk fibroin prepared from formic acid
    • Um I.C., Kweon H., Park Y.H., Hudson S. Structural characteristics and properties of the regenerated silk fibroin prepared from formic acid. Int. J. Biol. Macromol. 2001, 29:91-97.
    • (2001) Int. J. Biol. Macromol. , vol.29 , pp. 91-97
    • Um, I.C.1    Kweon, H.2    Park, Y.H.3    Hudson, S.4
  • 42
    • 0001673036 scopus 로고
    • Comparative studies of fibroins.2. Crystal structures of various fibroins
    • (350-&)
    • Warwicker J.O. Comparative studies of fibroins.2. Crystal structures of various fibroins. J. Mol. Biol. 1960, 2. (350-&).
    • (1960) J. Mol. Biol. , vol.2
    • Warwicker, J.O.1
  • 43
    • 84855844749 scopus 로고    scopus 로고
    • Milled cashmere guard hair powders: absorption properties to heavy metal ions
    • Patil K., Smith S.V., Rajkhowa R., Tsuzuki T., Wang X., Lin T. Milled cashmere guard hair powders: absorption properties to heavy metal ions. Powder Technol. 2012, 218:162-168.
    • (2012) Powder Technol. , vol.218 , pp. 162-168
    • Patil, K.1    Smith, S.V.2    Rajkhowa, R.3    Tsuzuki, T.4    Wang, X.5    Lin, T.6
  • 44
    • 77955167173 scopus 로고    scopus 로고
    • Silk fibroin/montmorillonite nanocomposites: effect of pH on the conformational transition and clay dispersion
    • Dang Q., Lu S., Yu S., Sun P., Yuan Z. Silk fibroin/montmorillonite nanocomposites: effect of pH on the conformational transition and clay dispersion. Biomacromolecules 2010, 11:1796-1801.
    • (2010) Biomacromolecules , vol.11 , pp. 1796-1801
    • Dang, Q.1    Lu, S.2    Yu, S.3    Sun, P.4    Yuan, Z.5
  • 45
    • 1942497564 scopus 로고
    • The distribution of chromium(VI) species in solution as a function of pH and concentration
    • Shen-Yang T., Ke-An L.I. The distribution of chromium(VI) species in solution as a function of pH and concentration. Talanta 1986, 33:775-777.
    • (1986) Talanta , vol.33 , pp. 775-777
    • Shen-Yang, T.1    Ke-An, L.I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.