메뉴 건너뛰기




Volumn 6, Issue , 2012, Pages 148-158

Micromechanical analysis of native and cross-linked collagen type I fibrils supports the existence of microfibrils

Author keywords

AFM (atomic force microscopy); Collagen; Mechanical properties; Microstructure

Indexed keywords

AFM; AFM (ATOMIC FORCE MICROSCOPY); AFM CANTILEVERS; COLLAGEN FIBRILS; COLLAGEN MOLECULES; COLLAGEN TYPE I; CROSS LINKING AGENTS; GLASS SURFACES; LINEAR REGION; MICRO-FIBRILS; MICRO-MECHANICAL ANALYSIS; MICROMECHANICAL BEHAVIOR; PRONY SERIES; RELAXATION MEASUREMENTS; STRESS-STRAIN BEHAVIORS; TENSILE TESTS; TOE REGION; VISCOELASTIC BEHAVIORS; VISCOELASTIC PROPERTIES;

EID: 83455211478     PISSN: 17516161     EISSN: 18780180     Source Type: Journal    
DOI: 10.1016/j.jmbbm.2011.11.008     Document Type: Article
Times cited : (88)

References (58)
  • 1
    • 4644294045 scopus 로고    scopus 로고
    • Flexibility of type I collagen and mechanical property of connective tissue
    • An K.N., Sun Y.L., Luo Z.P. Flexibility of type I collagen and mechanical property of connective tissue. Biorheology 2004, 41:239-246.
    • (2004) Biorheology , vol.41 , pp. 239-246
    • An, K.N.1    Sun, Y.L.2    Luo, Z.P.3
  • 2
    • 0027136085 scopus 로고
    • Subfibrillar structure of type I collagen observed by atomic force microscopy
    • Baselt D.R., Revel J.P., Baldeschwieler J.D. Subfibrillar structure of type I collagen observed by atomic force microscopy. Biophys. J. 1993, 65:2644-2655.
    • (1993) Biophys. J. , vol.65 , pp. 2644-2655
    • Baselt, D.R.1    Revel, J.P.2    Baldeschwieler, J.D.3
  • 3
    • 33747610222 scopus 로고    scopus 로고
    • Nature designs tough collagen: explaining the nanostructure of collagen fibrils
    • Buehler M.J. Nature designs tough collagen: explaining the nanostructure of collagen fibrils. Proc. Natl. Acad. Sci. USA 2006, 103:12285-12290.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 12285-12290
    • Buehler, M.J.1
  • 4
    • 35048874768 scopus 로고    scopus 로고
    • Nanomechanics of collagen fibrils under varying cross-link densities: atomistic and continuum studies
    • Buehler M.J. Nanomechanics of collagen fibrils under varying cross-link densities: atomistic and continuum studies. J. Mech. Behav. Biomed. Mater. 2008, 1:59-67.
    • (2008) J. Mech. Behav. Biomed. Mater. , vol.1 , pp. 59-67
    • Buehler, M.J.1
  • 5
    • 0022640049 scopus 로고
    • Comparison of material properties in fascicle-bone units from human patellar tendon and knee ligaments
    • Butler D.L., Kay M.D., Stouffer D.C. Comparison of material properties in fascicle-bone units from human patellar tendon and knee ligaments. J. Biomech. 1986, 19:425-432.
    • (1986) J. Biomech. , vol.19 , pp. 425-432
    • Butler, D.L.1    Kay, M.D.2    Stouffer, D.C.3
  • 7
    • 23944517971 scopus 로고    scopus 로고
    • Mechanical and functional properties of the equine superficial digital flexor tendon
    • Dowling B.A., Dart A.J. Mechanical and functional properties of the equine superficial digital flexor tendon. Vet. J. 2005, 170:184-192.
    • (2005) Vet. J. , vol.170 , pp. 184-192
    • Dowling, B.A.1    Dart, A.J.2
  • 8
    • 0030865343 scopus 로고    scopus 로고
    • Versatile collagens in invertebrates
    • Engel J. Versatile collagens in invertebrates. Science 1997, 277:1785-1786.
    • (1997) Science , vol.277 , pp. 1785-1786
    • Engel, J.1
  • 9
    • 33747122720 scopus 로고    scopus 로고
    • Nano measurements with micro-devices: mechanical properties of hydrated collagen fibrils
    • Eppell S.J., Smith B.N., Kahn H., Ballarini R. Nano measurements with micro-devices: mechanical properties of hydrated collagen fibrils. J. R. Soc. Interface 2006, 3:117-121.
    • (2006) J. R. Soc. Interface , vol.3 , pp. 117-121
    • Eppell, S.J.1    Smith, B.N.2    Kahn, H.3    Ballarini, R.4
  • 10
  • 13
    • 0000658473 scopus 로고
    • Quantitative analysis of the molecular sliding mechanism in native tendon collagen-time-resolved dynamic studies using synchrotron radiation
    • Folkhard W., Mosler E., Geercken W., Knörzer E., Nemetschek-Gansler H., Nemetschek Th., Koch M.H.J. Quantitative analysis of the molecular sliding mechanism in native tendon collagen-time-resolved dynamic studies using synchrotron radiation. Int. J. Biol. Macromol. 1987, 9:169-175.
    • (1987) Int. J. Biol. Macromol. , vol.9 , pp. 169-175
    • Folkhard, W.1    Mosler, E.2    Geercken, W.3    Knörzer, E.4    Nemetschek-Gansler, H.5    Nemetschek, T.6    Koch, M.H.J.7
  • 14
    • 79851488199 scopus 로고    scopus 로고
    • Hierarchical structure and nanomechanics of collagen microfibrils from the atomistic scale up
    • Gautieri A., Vesentini S., Redaelli A., Buehler M.J. Hierarchical structure and nanomechanics of collagen microfibrils from the atomistic scale up. Nano Lett. 2011, 11:757-766.
    • (2011) Nano Lett. , vol.11 , pp. 757-766
    • Gautieri, A.1    Vesentini, S.2    Redaelli, A.3    Buehler, M.J.4
  • 15
    • 4444296404 scopus 로고    scopus 로고
    • Structural changes in human type I collagen fibrils investigated by force spectroscopy
    • Graham J.S., Vomund A.N., Phillips C.L., Grandbois M. Structural changes in human type I collagen fibrils investigated by force spectroscopy. Exp. Cell Res. 2004, 299:335-342.
    • (2004) Exp. Cell Res. , vol.299 , pp. 335-342
    • Graham, J.S.1    Vomund, A.N.2    Phillips, C.L.3    Grandbois, M.4
  • 16
    • 33745674667 scopus 로고    scopus 로고
    • Exploring the mechanical properties of single vimentin intermediate filaments by atomic force microscopy
    • Guzmán C., Jeney S., Kreplak L., Kasas S., Kulik A.J., Aebi U., Forró L. Exploring the mechanical properties of single vimentin intermediate filaments by atomic force microscopy. J. Mol. Biol. 2006, 360:623-630.
    • (2006) J. Mol. Biol. , vol.360 , pp. 623-630
    • Guzmán, C.1    Jeney, S.2    Kreplak, L.3    Kasas, S.4    Kulik, A.J.5    Aebi, U.6    Forró, L.7
  • 17
    • 0036427708 scopus 로고    scopus 로고
    • In situ force microscopy of partially demineralized human dentin collagen fibrils
    • Habelitz S., Balooch M., Marshall S.J., Balooch G., Marshall G.W. In situ force microscopy of partially demineralized human dentin collagen fibrils. J. Struct. Biol. 2002, 138:227-236.
    • (2002) J. Struct. Biol. , vol.138 , pp. 227-236
    • Habelitz, S.1    Balooch, M.2    Marshall, S.J.3    Balooch, G.4    Marshall, G.W.5
  • 18
    • 0031060035 scopus 로고    scopus 로고
    • The state of tissue hydration determines the strain-rate-sensitive stiffness of human patellar tendon
    • Haut T.L., Haut R.C. The state of tissue hydration determines the strain-rate-sensitive stiffness of human patellar tendon. J. Biomech. 1997, 30:79-81.
    • (1997) J. Biomech. , vol.30 , pp. 79-81
    • Haut, T.L.1    Haut, R.C.2
  • 19
    • 0035912751 scopus 로고    scopus 로고
    • Corneal collagen fibril structure in three dimensions: structural insights into fibril assembly, mechanical properties, and tissue organization
    • Holmes D.F., Gilpin C.J., Baldock C., Ziese U., Koster A.J., Kadler K.E. Corneal collagen fibril structure in three dimensions: structural insights into fibril assembly, mechanical properties, and tissue organization. Proc. Natl. Acad. Sci. USA 2001, 98:7307-7312.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7307-7312
    • Holmes, D.F.1    Gilpin, C.J.2    Baldock, C.3    Ziese, U.4    Koster, A.J.5    Kadler, K.E.6
  • 20
    • 0036447070 scopus 로고    scopus 로고
    • Building collagen molecules, fibrils, and suprafibrillar structures
    • Hulmes D.J.S. Building collagen molecules, fibrils, and suprafibrillar structures. J. Struct. Biol. 2002, 137:2-10.
    • (2002) J. Struct. Biol. , vol.137 , pp. 2-10
    • Hulmes, D.J.S.1
  • 22
    • 4143116694 scopus 로고    scopus 로고
    • Effects of age on the stress-strain and stress-relaxation properties of the rat molar periodontal ligament
    • Komatsu K., Kanazashi M., Shimada A., Shibata T., Viidik A., Chiba M. Effects of age on the stress-strain and stress-relaxation properties of the rat molar periodontal ligament. Arch. Oral Biol. 2004, 49:817-824.
    • (2004) Arch. Oral Biol. , vol.49 , pp. 817-824
    • Komatsu, K.1    Kanazashi, M.2    Shimada, A.3    Shibata, T.4    Viidik, A.5    Chiba, M.6
  • 23
    • 0142139178 scopus 로고    scopus 로고
    • Effect of fiber orientation and strain rate on the nonlinear uniaxial tensile material properties of tendon
    • Lynch H.A., Johannessen W., Wu J.P., Jawa A., Elliott D.M. Effect of fiber orientation and strain rate on the nonlinear uniaxial tensile material properties of tendon. J. Biomech. Eng. 2003, 125:726-731.
    • (2003) J. Biomech. Eng. , vol.125 , pp. 726-731
    • Lynch, H.A.1    Johannessen, W.2    Wu, J.P.3    Jawa, A.4    Elliott, D.M.5
  • 24
    • 0344873751 scopus 로고    scopus 로고
    • Tendon properties in relation to muscular activity and physical training
    • Magnusson S.P., Hansen P., Kjaer M. Tendon properties in relation to muscular activity and physical training. Scand. J. Med. Sci. Sports 2003, 13:211-223.
    • (2003) Scand. J. Med. Sci. Sports , vol.13 , pp. 211-223
    • Magnusson, S.P.1    Hansen, P.2    Kjaer, M.3
  • 25
    • 0031041821 scopus 로고    scopus 로고
    • A new molecular model for collagen elasticity based on synchrotron X-ray scattering evidence
    • Misof K., Rapp G., Fratzl P. A new molecular model for collagen elasticity based on synchrotron X-ray scattering evidence. Biophys. J. 1997, 72:1376-1381.
    • (1997) Biophys. J. , vol.72 , pp. 1376-1381
    • Misof, K.1    Rapp, G.2    Fratzl, P.3
  • 29
    • 3042606295 scopus 로고    scopus 로고
    • Measurement of hardness and elastic modulus by instrumented indentation: advances in understanding and refinement to methodology
    • Oliver W.C., Pharr G.M. Measurement of hardness and elastic modulus by instrumented indentation: advances in understanding and refinement to methodology. J. Mater. Res. 2004, 19:3-20.
    • (2004) J. Mater. Res. , vol.19 , pp. 3-20
    • Oliver, W.C.1    Pharr, G.M.2
  • 32
    • 0006696584 scopus 로고
    • A self-assembled collagen scaffold suitable for use in soft and hard tissue replacement
    • Pins G.D., Silver F.H. A self-assembled collagen scaffold suitable for use in soft and hard tissue replacement. Mater. Sci. Eng. C 1995, 3:101-107.
    • (1995) Mater. Sci. Eng. C , vol.3 , pp. 101-107
    • Pins, G.D.1    Silver, F.H.2
  • 35
    • 0035197704 scopus 로고    scopus 로고
    • Tapping-mode atomic force microscopy in fluid of hydrated extracellular matrix
    • Raspanti M., Congiu T., Guizzardi S. Tapping-mode atomic force microscopy in fluid of hydrated extracellular matrix. Matrix Biol. 2001, 20:601-604.
    • (2001) Matrix Biol. , vol.20 , pp. 601-604
    • Raspanti, M.1    Congiu, T.2    Guizzardi, S.3
  • 36
    • 2442517329 scopus 로고    scopus 로고
    • Strain-rate sensitive mechanical properties of tendon fascicles from mice with genetically engineered alterations in collagen and decorin
    • Robinson P.S., Lin T.W., Reynolds P.R., Derwin K.A., Iozzo R.V., Soslowsky L.J. Strain-rate sensitive mechanical properties of tendon fascicles from mice with genetically engineered alterations in collagen and decorin. J. Biomech. Eng. 2004, 126:252-257.
    • (2004) J. Biomech. Eng. , vol.126 , pp. 252-257
    • Robinson, P.S.1    Lin, T.W.2    Reynolds, P.R.3    Derwin, K.A.4    Iozzo, R.V.5    Soslowsky, L.J.6
  • 37
    • 0030246115 scopus 로고    scopus 로고
    • Elongation mechanism of collagen fibrils and force-strain relations of tendon at each level of structural hierarchy
    • Sasaki N., Odajima S. Elongation mechanism of collagen fibrils and force-strain relations of tendon at each level of structural hierarchy. J. Biomech. 1996, 29:1131-1136.
    • (1996) J. Biomech. , vol.29 , pp. 1131-1136
    • Sasaki, N.1    Odajima, S.2
  • 38
    • 8644258535 scopus 로고    scopus 로고
    • An investigation into the effects of the hierarchical structure of tendon fascicles on micromechanical properties
    • Screen H.R.C., Lee D.A., Bader D.L., Shelton J.C. An investigation into the effects of the hierarchical structure of tendon fascicles on micromechanical properties. Proc. Inst. Mech. Eng. H. 2004, 218:109-119.
    • (2004) Proc. Inst. Mech. Eng. H. , vol.218 , pp. 109-119
    • Screen, H.R.C.1    Lee, D.A.2    Bader, D.L.3    Shelton, J.C.4
  • 40
    • 79960292996 scopus 로고    scopus 로고
    • Viscoelastic properties of isolated collagen fibrils
    • Shen Z.L., Kahn H., Ballarini R., Eppell S.J. Viscoelastic properties of isolated collagen fibrils. Biophys. J. 2011, 100:3008-3015.
    • (2011) Biophys. J. , vol.100 , pp. 3008-3015
    • Shen, Z.L.1    Kahn, H.2    Ballarini, R.3    Eppell, S.J.4
  • 42
    • 0141453852 scopus 로고    scopus 로고
    • Collagen self-assembly and the development of tendon mechanical properties
    • Silver F.H., Freeman J.W., Seehra G.P. Collagen self-assembly and the development of tendon mechanical properties. J. Biomech. 2003, 36:1529-1553.
    • (2003) J. Biomech. , vol.36 , pp. 1529-1553
    • Silver, F.H.1    Freeman, J.W.2    Seehra, G.P.3
  • 43
    • 0014412958 scopus 로고
    • Molecular pattern in native collagen
    • Smith J.W. Molecular pattern in native collagen. Nature 1968, 219:157-158.
    • (1968) Nature , vol.219 , pp. 157-158
    • Smith, J.W.1
  • 46
    • 78650205939 scopus 로고    scopus 로고
    • Tensile properties of human collagen fibrils and fascicles are insensitive to environmental salts
    • Svennson R.B., Hassenkam T., Grant C.A., Magnusson S.P. Tensile properties of human collagen fibrils and fascicles are insensitive to environmental salts. Biophys. J. 2010, 99:4020-4027.
    • (2010) Biophys. J. , vol.99 , pp. 4020-4027
    • Svennson, R.B.1    Hassenkam, T.2    Grant, C.A.3    Magnusson, S.P.4
  • 49
    • 0001026801 scopus 로고    scopus 로고
    • A method for determining the spring constant of cantilevers for atomic force microscopy
    • Torii A., Sasaki M., Hane K., Okuma S. A method for determining the spring constant of cantilevers for atomic force microscopy. Meas. Sci. Technol. 1996, 7:179-184.
    • (1996) Meas. Sci. Technol. , vol.7 , pp. 179-184
    • Torii, A.1    Sasaki, M.2    Hane, K.3    Okuma, S.4
  • 50
    • 0347241157 scopus 로고    scopus 로고
    • Role of secondary structure on the stress relaxation processes in rat tail tendon (RTT) collagen fibre
    • Usha R., Subramaniam V., Ramasami T. Role of secondary structure on the stress relaxation processes in rat tail tendon (RTT) collagen fibre. Macromol. Biosci. 2001, 1:100-107.
    • (2001) Macromol. Biosci. , vol.1 , pp. 100-107
    • Usha, R.1    Subramaniam, V.2    Ramasami, T.3
  • 52
    • 33745439465 scopus 로고    scopus 로고
    • Mechanobiology of tendon
    • Wang J.H.C. Mechanobiology of tendon. J. Biomech. 2006, 39:1563-1582.
    • (2006) J. Biomech. , vol.39 , pp. 1563-1582
    • Wang, J.H.C.1
  • 55
    • 33750744051 scopus 로고    scopus 로고
    • Quantitative constitutive behaviour and viscoelastic properties of fresh flexor tendons
    • Wu J.J. Quantitative constitutive behaviour and viscoelastic properties of fresh flexor tendons. Int. J. Artif. Organs 2006, 29:852-857.
    • (2006) Int. J. Artif. Organs , vol.29 , pp. 852-857
    • Wu, J.J.1
  • 56
    • 30844469311 scopus 로고    scopus 로고
    • Estimation of the viscous properties of skin and subcutaneous tissue in uniaxial stress relaxation tests
    • Wu J.Z., Cutlip R.G., Welcome D., Dong R.G. Estimation of the viscous properties of skin and subcutaneous tissue in uniaxial stress relaxation tests. Biomed. Mater. Eng. 2006, 16:53-66.
    • (2006) Biomed. Mater. Eng. , vol.16 , pp. 53-66
    • Wu, J.Z.1    Cutlip, R.G.2    Welcome, D.3    Dong, R.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.