메뉴 건너뛰기




Volumn 10, Issue 6, 2015, Pages

Fabrication of homobifunctional crosslinker stabilized collagen for biomedical application

Author keywords

collagen stabilization; crosslinking; mechanical property; thermal stability

Indexed keywords

BIOMECHANICS; CROSSLINKING; ELASTIC MODULI; ETHYLENE; ETHYLENE GLYCOL; MECHANICAL PROPERTIES; MECHANICAL STABILITY; MEDICAL APPLICATIONS; SHEAR STRESS; STABILIZATION; TENSILE STRENGTH; TENSILE TESTING; THERMODYNAMIC STABILITY; THERMOGRAVIMETRIC ANALYSIS; TISSUE; TISSUE ENGINEERING;

EID: 84950119540     PISSN: 17486041     EISSN: 1748605X     Source Type: Journal    
DOI: 10.1088/1748-6041/10/6/065015     Document Type: Article
Times cited : (12)

References (39)
  • 1
    • 84877651655 scopus 로고    scopus 로고
    • Organisation of collagen in the presence of diphenyl phosphoryl azide (DPPA): An in vitro study
    • Organisation of collagen in the presence of diphenyl phosphoryl azide (DPPA): an in vitro study 121-8
    • Usha R, Sreeram K J and Mandal A B 2013 Organisation of collagen in the presence of diphenyl phosphoryl azide (DPPA): an in vitro study Colloids Surf. B 109 121-8
    • (2013) Colloids Surf. , vol.109 , pp. 121-128
    • Usha, R.1    Sreeram, K.J.2    Mandal, A.B.3
  • 2
    • 66249091230 scopus 로고    scopus 로고
    • Cross-linking of extruded collagen fibers - A biomimetic three-dimensional scaffold for tissue engineering applications
    • 895-908
    • Zeugolis D I, Paul G R and Attenburrow G 2011 Cross-linking of extruded collagen fibers - a biomimetic three-dimensional scaffold for tissue engineering applications J. Biomed. Mater. Res. A 89 895-908
    • (2011) J. Biomed. Mater. Res. , vol.89 , pp. 895-908
    • Zeugolis, D.I.1    Paul, G.R.2    Attenburrow, G.3
  • 3
    • 79959821866 scopus 로고    scopus 로고
    • Properties of alkali-solubilized collagen solution crosslinked by N-hydroxysuccinimide activated adipic acid
    • 41-8
    • Chen Y, Zhang M, Liu W and Li G 2009 Properties of alkali-solubilized collagen solution crosslinked by N-hydroxysuccinimide activated adipic acid Korea-Australia Rheol. J. 23 41-8
    • (2009) Korea-Australia Rheol. J. , vol.23 , Issue.1 , pp. 41-48
    • Chen, Y.1    Zhang, M.2    Liu, W.3    Li, G.4
  • 4
    • 84877086335 scopus 로고    scopus 로고
    • Naturally and synthetic smart composite biomaterials for tissue regeneration
    • 471-96
    • Pérez R A, Won J E, Knowles J C and Kim H W 2013 Naturally and synthetic smart composite biomaterials for tissue regeneration Adv. Drug Deliv. Rev. 65 471-96
    • (2013) Adv. Drug Deliv. Rev. , vol.65 , pp. 471-496
    • Pérez, R.A.1    Won, J.E.2    Knowles, J.C.3    Kim, H.W.4
  • 6
    • 79957625010 scopus 로고    scopus 로고
    • Collagen-based biomaterials for tissue engineering applications
    • 1863-87
    • Bareil R P, Gauvin R and Berthod F 2010 Collagen-based biomaterials for tissue engineering applications Materials 3 1863-87
    • (2010) Materials , vol.3 , Issue.3 , pp. 1863-1887
    • Bareil, R.P.1    Gauvin, R.2    Berthod, F.3
  • 7
    • 80051668474 scopus 로고    scopus 로고
    • Collagen stabilization and modification using a polyepoxide, triglycidyl isocyanurate
    • 1684-92
    • Di Y and Heath R J 2009 Collagen stabilization and modification using a polyepoxide, triglycidyl isocyanurate Polym. Degrad. Stab. 94 1684-92
    • (2009) Polym. Degrad. Stab. , vol.94 , Issue.10 , pp. 1684-1692
    • Di, Y.1    Heath, R.J.2
  • 8
    • 48249091315 scopus 로고    scopus 로고
    • Role of solvents in stability of collagen
    • 541-5
    • Usha R and Ramasami T 2008 Role of solvents in stability of collagen J. Therm. Anal. Calorim. 93 541-5
    • (2008) J. Therm. Anal. Calorim. , vol.93 , pp. 541-545
    • Usha, R.1    Ramasami, T.2
  • 9
    • 0035118457 scopus 로고    scopus 로고
    • Thermal stability of collagen fibers in ethylene glycol
    • 1480-6
    • Miles C A and Burjanadze T V 2001 Thermal stability of collagen fibers in ethylene glycol Biophys. J. 80 1480-6
    • (2001) Biophys. J. , vol.80 , pp. 1480-1486
    • Miles, C.A.1    Burjanadze, T.V.2
  • 10
    • 80052299542 scopus 로고    scopus 로고
    • Interactions of collagen molecules in the presence of N-hydroxysuccinimide activated adipic acid (NHS-AA) as a crosslinking agent
    • Interactions of collagen molecules in the presence of N-hydroxysuccinimide activated adipic acid (NHS-AA) as a crosslinking agent 847-54
    • Zhang M, Wu K and Li G 2011 Interactions of collagen molecules in the presence of N-hydroxysuccinimide activated adipic acid (NHS-AA) as a crosslinking agent Int. J. Biol. Macromol. 49 847-54
    • (2011) Int. J. Biol. Macromol. , vol.49 , pp. 847-854
    • Zhang, M.1    Wu, K.2    Li, G.3
  • 12
    • 0032192113 scopus 로고    scopus 로고
    • A novel surgical glue composed of gelatin and N-hydroxysuccinimide activated poly(L-glutamic acid): Part 1. Synthesis of activated poly(L-glutamic acid) and its gelation with gelatin
    • A novel surgical glue composed of gelatin and N-hydroxysuccinimide activated poly(L-glutamic acid): part 1. Synthesis of activated poly(L-glutamic acid) and its gelation with gelatin 1869-76
    • Iwata H, Matsuda S, Mitsuhashi K, Itoh E and Ikada Y 1998 A novel surgical glue composed of gelatin and N-hydroxysuccinimide activated poly(L-glutamic acid): part 1. Synthesis of activated poly(L-glutamic acid) and its gelation with gelatin Biomaterials 19 1869-76
    • (1998) Biomaterials , vol.19 , pp. 1869-1876
    • Iwata, H.1    Matsuda, S.2    Mitsuhashi, K.3    Itoh, E.4    Ikada, Y.5
  • 13
    • 9444285532 scopus 로고    scopus 로고
    • Rheological evaluation of gelatin gels prepared with a citric acid derivative as a novel cross-linker
    • 787-90
    • Aoki H, Taguchi T, Saito H, Kobayashi H, Kataoka K and Tanaka J 2004 Rheological evaluation of gelatin gels prepared with a citric acid derivative as a novel cross-linker Mater. Sci. Eng. C 24 787-90
    • (2004) Mater. Sci. Eng. , vol.24 , pp. 787-790
    • Aoki, H.1    Taguchi, T.2    Saito, H.3    Kobayashi, H.4    Kataoka, K.5    Tanaka, J.6
  • 14
    • 33751307196 scopus 로고    scopus 로고
    • PH-responsive swelling behavior of collagen gels prepared by novel crosslinkers based on naturally derived di- or tricarboxylic acids
    • 89-94
    • Saito H, Taguchi T, Aoki H, Murabayashi S, Mitamura Y, Tanaka J and Tateishi T 2007 pH-responsive swelling behavior of collagen gels prepared by novel crosslinkers based on naturally derived di- or tricarboxylic acids Acta Biomater. 3 89-94
    • (2007) Acta Biomater. , vol.3 , pp. 89-94
    • Saito, H.1    Taguchi, T.2    Aoki, H.3    Murabayashi, S.4    Mitamura, Y.5    Tanaka, J.6    Tateishi, T.7
  • 15
    • 9444244377 scopus 로고    scopus 로고
    • Study on the hydrolytic degradation of poly (α, β-malic acid) by direct polycondensation
    • Study on the hydrolytic degradation of poly (alpha;, beta;-malic acid) by direct polycondensation 821-5
    • Kajiyama T, Kobayashi H, Taguchi T, Komatsu Y, Kataoka K and Tanaka J 2004 Study on the hydrolytic degradation of poly (α, β-malic acid) by direct polycondensation Mater. Sci. Eng. C 24 821-5
    • (2004) Mater. Sci. Eng. , vol.24 , pp. 821-825
    • Kajiyama, T.1    Kobayashi, H.2    Taguchi, T.3    Komatsu, Y.4    Kataoka, K.5    Tanaka, J.6
  • 16
    • 0018407815 scopus 로고
    • A new cleavable reagent for cross linking and reversible immobilization of proteins
    • 734-42
    • Abdella P M, Smith P K and Royer G P 1979 A new cleavable reagent for cross linking and reversible immobilization of proteins Biochem. Biophys. Res. Commun. 87 734-42
    • (1979) Biochem. Biophys. Res. Commun. , vol.87 , pp. 734-742
    • Abdella, P.M.1    Smith, P.K.2    Royer, G.P.3
  • 17
    • 24044520965 scopus 로고    scopus 로고
    • Isotopically coded cleavable cross-linker for studying protein-protein interaction and protein complexes
    • 1167-79
    • Petrotchenko E V, Olkhovik V K and Borchers C H 2005 Isotopically coded cleavable cross-linker for studying protein-protein interaction and protein complexes Mol. Cell Proteomics 4 1167-79
    • (2005) Mol. Cell Proteomics , vol.4 , pp. 1167-1179
    • Petrotchenko, E.V.1    Olkhovik, V.K.2    Borchers, C.H.3
  • 18
    • 0035134624 scopus 로고    scopus 로고
    • Studies on Rana tigerina skin collagen
    • 81-90
    • Sai K P and Babu M 2001 Studies on Rana tigerina skin collagen Comput. Biochem. Physiol. B 128 81-90
    • (2001) Comput. Biochem. Physiol. , vol.128 , pp. 81-90
    • Sai, K.P.1    Babu, M.2
  • 19
    • 33745996622 scopus 로고
    • The determination of hydroxyproline in tissue and protein samples containing small proportions of this imino acid
    • Woessner J F Jr 440-7
    • Woessner J F Jr 1961 The determination of hydroxyproline in tissue and protein samples containing small proportions of this imino acid Arch. Biochem. Biophys. 93 440-7
    • (1961) Arch. Biochem. Biophys. , vol.93 , pp. 440-447
    • Woessner, J.F.1
  • 20
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assay
    • 55-63
    • Mosmann T 1983 Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assay J. Immunol. Methods 55 55-63
    • (1983) J. Immunol. Methods , vol.55 , pp. 55-63
    • Mosmann, T.1
  • 21
    • 0026614994 scopus 로고
    • The determination of epsilon-amino groups in soluble and poorly soluble proteinaceous materials by a spectrophotometric method using trinitrobenzenesulfonic acid
    • 129-33
    • Bubnis W A and Ofner C M 1992 The determination of epsilon-amino groups in soluble and poorly soluble proteinaceous materials by a spectrophotometric method using trinitrobenzenesulfonic acid Anal. Biochem. 207 129-33
    • (1992) Anal. Biochem. , vol.207 , pp. 129-133
    • Bubnis, W.A.1    Ofner, C.M.2
  • 23
    • 15944420546 scopus 로고    scopus 로고
    • Characterization of collagen matrices crosslinked using microbial transglutaminase
    • 4229-35
    • Chen R N, Ho H O and Sheu M T 2005 Characterization of collagen matrices crosslinked using microbial transglutaminase Biomaterials 26 4229-35
    • (2005) Biomaterials , vol.26 , pp. 4229-4235
    • Chen, R.N.1    Ho, H.O.2    Sheu, M.T.3
  • 24
    • 84863213613 scopus 로고    scopus 로고
    • Crosslinking and composition influence the surface properties, mechanical stiffness and cell reactivity of collagen-based films
    • 3080-90
    • Grover C N, Gwynne J H, Pugh N, Hamaia S, Farndale R W, Best S M and Cameron R E 2012 Crosslinking and composition influence the surface properties, mechanical stiffness and cell reactivity of collagen-based films Acta Biomater. 8 3080-90
    • (2012) Acta Biomater. , vol.8 , pp. 3080-3090
    • Grover, C.N.1    Gwynne, J.H.2    Pugh, N.3    Hamaia, S.4    Farndale, R.W.5    Best, S.M.6    Cameron, R.E.7
  • 25
    • 0018079235 scopus 로고
    • Collagen fibril formation. Optimal in vitro conditions and preliminary kinetic results
    • 6578-85
    • Williams B R, Gelman R A, Poppke D C and Piez K A 1978 Collagen fibril formation. Optimal in vitro conditions and preliminary kinetic results J. Biol. Chem. 253 6578-85
    • (1978) J. Biol. Chem. , vol.253 , pp. 6578-6585
    • Williams, B.R.1    Gelman, R.A.2    Poppke, D.C.3    Piez, K.A.4
  • 26
    • 0001358434 scopus 로고
    • The formation of fibrils from collagen solutions. A mechanism of collagen fibril formation
    • 598-605
    • Wood G C 1960 The formation of fibrils from collagen solutions. A mechanism of collagen fibril formation Biochem. J. 75 598-605
    • (1960) Biochem. J. , vol.75 , pp. 598-605
    • Wood, G.C.1
  • 27
    • 67349124784 scopus 로고    scopus 로고
    • PH effects on collagen fibrillogenesis in vitro: Electrostatic interactions and phosphate binding
    • 1643-9
    • Li Y, Asadi A, Monroe M R and Douglas E P 2009 pH effects on collagen fibrillogenesis in vitro: electrostatic interactions and phosphate binding Mater. Sci. Eng. C 29 1643-9
    • (2009) Mater. Sci. Eng. , vol.29 , pp. 1643-1649
    • Li, Y.1    Asadi, A.2    Monroe, M.R.3    Douglas, E.P.4
  • 28
    • 85003043864 scopus 로고    scopus 로고
    • Understanding the viscoelastic behavior of collagen matrices through relaxation time distribution spectrum
    • Xu B, Li H and Zhang Y 2013 Understanding the viscoelastic behavior of collagen matrices through relaxation time distribution spectrum Biomatter 3 e24651
    • (2013) Biomatter , vol.3
    • Xu, B.1    Li, H.2    Zhang, Y.3
  • 29
    • 2142815834 scopus 로고    scopus 로고
    • Comparative physico-chemical and in vitro properties of fibrillated collagen scaffolds from different sources
    • 247-64
    • Shanmugasundaram N, Ravikumar T and Babu M 2004 Comparative physico-chemical and in vitro properties of fibrillated collagen scaffolds from different sources J. Biomater. Appl. 18 247-64
    • (2004) J. Biomater. Appl. , vol.18 , pp. 247-264
    • Shanmugasundaram, N.1    Ravikumar, T.2    Babu, M.3
  • 30
    • 10744232100 scopus 로고    scopus 로고
    • Influence of different collagen species on physico-chemical properties of crosslinked collagen matrices
    • 2831-41
    • Angele P et al 2004 Influence of different collagen species on physico-chemical properties of crosslinked collagen matrices Biomaterials 25 2831-41
    • (2004) Biomaterials , vol.25 , pp. 2831-2841
    • Angele, P.1
  • 31
  • 32
    • 72049102340 scopus 로고    scopus 로고
    • Chemico-physical characterization of gelatin films modified with oxidized alginate
    • 383-8
    • Boanini E, Rubini K, Panzavolta S and Bigi A 2010 Chemico-physical characterization of gelatin films modified with oxidized alginate Acta Biomater. 6 383-8
    • (2010) Acta Biomater. , vol.6 , pp. 383-388
    • Boanini, E.1    Rubini, K.2    Panzavolta, S.3    Bigi, A.4
  • 33
    • 67650035187 scopus 로고    scopus 로고
    • Fabrication and characterization of aligned nanofibrous PLGA/collagen blends as bone tissue scaffolds
    • 3778-85
    • Jose M V, Thomas V, Dean D R and Nyairo E 2009 Fabrication and characterization of aligned nanofibrous PLGA/collagen blends as bone tissue scaffolds Polymer 50 3778-85
    • (2009) Polymer , vol.50 , pp. 3778-3785
    • Jose, M.V.1    Thomas, V.2    Dean, D.R.3    Nyairo, E.4
  • 34
    • 82355191679 scopus 로고    scopus 로고
    • Stabilization of collagen with EDC/NHS in the presence of L-lysine: A comprehensive study
    • 83-90
    • Usha R, Sreeram K J and Rajaram A 2012 Stabilization of collagen with EDC/NHS in the presence of L-lysine: a comprehensive study Colloids Surf. B 90 83-90
    • (2012) Colloids Surf. , vol.90 , pp. 83-90
    • Usha, R.1    Sreeram, K.J.2    Rajaram, A.3
  • 36
    • 33846292554 scopus 로고    scopus 로고
    • Mechanical properties of gelatin films cross-linked, respectively, by ferulic acid and tannin acid
    • 575-84
    • Cao N, Fu Y and He J 2007 Mechanical properties of gelatin films cross-linked, respectively, by ferulic acid and tannin acid Food Hydrocolloids 21 575-84
    • (2007) Food Hydrocolloids , vol.21 , pp. 575-584
    • Cao, N.1    Fu, Y.2    He, J.3
  • 37
    • 33644833756 scopus 로고    scopus 로고
    • Photochemical crosslinking improves the physicochemical properties of collagen scaffolds
    • 689-701
    • Chan B P and So K F 2005 Photochemical crosslinking improves the physicochemical properties of collagen scaffolds J. Biomed. Mater. Res. A 75A 689-701
    • (2005) J. Biomed. Mater. Res. , vol.75 , pp. 689-701
    • Chan, B.P.1    So, K.F.2
  • 38
    • 1142309724 scopus 로고    scopus 로고
    • Enhanced biological stability of collagen porous scaffolds by using amino acids as novel cross-linking bridges
    • 2997-3004
    • Ma L, Gao C, Mao Z, Zhou J and Shen J 2004 Enhanced biological stability of collagen porous scaffolds by using amino acids as novel cross-linking bridges Biomaterials 25 2997-3004
    • (2004) Biomaterials , vol.25 , pp. 2997-3004
    • Ma, L.1    Gao, C.2    Mao, Z.3    Zhou, J.4    Shen, J.5
  • 39
    • 84868259478 scopus 로고    scopus 로고
    • Enhanced physicochemical properties of collagen by using EDC/NHS-crosslinking
    • 913-8
    • Yang C 2012 Enhanced physicochemical properties of collagen by using EDC/NHS-crosslinking Bull. Mater. Sci. 35 913-8
    • (2012) Bull. Mater. Sci. , vol.35 , pp. 913-918
    • Yang, C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.