Micromechanical analysis of native and cross-linked collagen type 1 fibrils supports the existence of microfibrils

Lanti Yang, Kees van der Werf, Pieter J. Dijkstra, Jan Feijen, Martin L. Bennink

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Abstract

The mechanical properties of individual collagen fibrils of approximately 200 nm in diameter were determined using a slightly adapted AFM system. Single collagen fibrils immersed in PBS buffer were attached between an AFM cantilever and a glass surface to perform tensile tests at different strain rates and stress relaxation measurements. The stress–strain behavior of collagen fibrils immersed in PBS buffer comprises a toe region up to a stress of 5 MPa, followed by the heel and linear region at higher stresses. Hysteresis and strain-rate dependent stress–strain behavior of collagen fibrils were observed, which suggest that single collagen fibrils have viscoelastic properties. The stress relaxation process of individual collagen fibrils could be best fitted using a two-term Prony series. Furthermore, the influence of different cross-linking agents on the mechanical properties of single collagen fibrils was investigated. Based on these results, we propose that sliding of microfibrils with respect to each other plays a role in the viscoelastic behavior of collagen fibrils in addition to the sliding of collagen molecules with respect to each other. Our finding provides a better insight into the relationship between the structure and mechanical properties of collagen and the micro-mechanical behavior of tissues
Original languageEnglish
Pages (from-to)148-158
Number of pages11
JournalJournal of the mechanical behavior of biomedical materials
Volume6
DOIs
Publication statusPublished - 2012

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Collagen Type I
Collagen
Stress relaxation
Mechanical properties
Strain rate
Buffers
Relaxation processes
Hysteresis
Tissue
Glass
Molecules

Keywords

  • METIS-290428
  • IR-83151

Cite this

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title = "Micromechanical analysis of native and cross-linked collagen type 1 fibrils supports the existence of microfibrils",
abstract = "The mechanical properties of individual collagen fibrils of approximately 200 nm in diameter were determined using a slightly adapted AFM system. Single collagen fibrils immersed in PBS buffer were attached between an AFM cantilever and a glass surface to perform tensile tests at different strain rates and stress relaxation measurements. The stress–strain behavior of collagen fibrils immersed in PBS buffer comprises a toe region up to a stress of 5 MPa, followed by the heel and linear region at higher stresses. Hysteresis and strain-rate dependent stress–strain behavior of collagen fibrils were observed, which suggest that single collagen fibrils have viscoelastic properties. The stress relaxation process of individual collagen fibrils could be best fitted using a two-term Prony series. Furthermore, the influence of different cross-linking agents on the mechanical properties of single collagen fibrils was investigated. Based on these results, we propose that sliding of microfibrils with respect to each other plays a role in the viscoelastic behavior of collagen fibrils in addition to the sliding of collagen molecules with respect to each other. Our finding provides a better insight into the relationship between the structure and mechanical properties of collagen and the micro-mechanical behavior of tissues",
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author = "Lanti Yang and {van der Werf}, Kees and Dijkstra, {Pieter J.} and Jan Feijen and Bennink, {Martin L.}",
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doi = "10.1016/j.jmbbm.2011.11.008",
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journal = "Journal of the mechanical behavior of biomedical materials",
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T1 - Micromechanical analysis of native and cross-linked collagen type 1 fibrils supports the existence of microfibrils

AU - Yang, Lanti

AU - van der Werf, Kees

AU - Dijkstra, Pieter J.

AU - Feijen, Jan

AU - Bennink, Martin L.

PY - 2012

Y1 - 2012

N2 - The mechanical properties of individual collagen fibrils of approximately 200 nm in diameter were determined using a slightly adapted AFM system. Single collagen fibrils immersed in PBS buffer were attached between an AFM cantilever and a glass surface to perform tensile tests at different strain rates and stress relaxation measurements. The stress–strain behavior of collagen fibrils immersed in PBS buffer comprises a toe region up to a stress of 5 MPa, followed by the heel and linear region at higher stresses. Hysteresis and strain-rate dependent stress–strain behavior of collagen fibrils were observed, which suggest that single collagen fibrils have viscoelastic properties. The stress relaxation process of individual collagen fibrils could be best fitted using a two-term Prony series. Furthermore, the influence of different cross-linking agents on the mechanical properties of single collagen fibrils was investigated. Based on these results, we propose that sliding of microfibrils with respect to each other plays a role in the viscoelastic behavior of collagen fibrils in addition to the sliding of collagen molecules with respect to each other. Our finding provides a better insight into the relationship between the structure and mechanical properties of collagen and the micro-mechanical behavior of tissues

AB - The mechanical properties of individual collagen fibrils of approximately 200 nm in diameter were determined using a slightly adapted AFM system. Single collagen fibrils immersed in PBS buffer were attached between an AFM cantilever and a glass surface to perform tensile tests at different strain rates and stress relaxation measurements. The stress–strain behavior of collagen fibrils immersed in PBS buffer comprises a toe region up to a stress of 5 MPa, followed by the heel and linear region at higher stresses. Hysteresis and strain-rate dependent stress–strain behavior of collagen fibrils were observed, which suggest that single collagen fibrils have viscoelastic properties. The stress relaxation process of individual collagen fibrils could be best fitted using a two-term Prony series. Furthermore, the influence of different cross-linking agents on the mechanical properties of single collagen fibrils was investigated. Based on these results, we propose that sliding of microfibrils with respect to each other plays a role in the viscoelastic behavior of collagen fibrils in addition to the sliding of collagen molecules with respect to each other. Our finding provides a better insight into the relationship between the structure and mechanical properties of collagen and the micro-mechanical behavior of tissues

KW - METIS-290428

KW - IR-83151

U2 - 10.1016/j.jmbbm.2011.11.008

DO - 10.1016/j.jmbbm.2011.11.008

M3 - Article

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SP - 148

EP - 158

JO - Journal of the mechanical behavior of biomedical materials

JF - Journal of the mechanical behavior of biomedical materials

SN - 1751-6161

ER -