TY - JOUR

T1 - Glutaraldehyde cross-linking of tendon mechanical effects at the level of the tendon fascicle and fibril

AU - Hansen, Philip

AU - Hassenkam, Tue

AU - Svensson, Rene Bruggebusch

AU - Aagaard, Per

AU - Trappe, Todd

AU - Haraldsson, Bjarki Thor

AU - Kjaer, Michael

AU - Magnusson, Peter

PY - 2009

Y1 - 2009

N2 - Conclusive insight into the microscopic principles that govern the strength of tendon and related connective tissues is lacking and the importance of collagen cross-linking has not been firmly established. The combined application of whole-tissue mechanical testing and atomic force spectroscopy allowed for a detailed characterization of the effect of cross-linking in rat-tail tendon. The cross-link inducing agent glutaraldehyde augmented the tensile strength of tendon fascicles. Stress at failure increased from approximately 8 MPa to approximately 39 MPa. The mechanical effects of glutaraldehyde at the tendon fibril level were examined by atomic force microscopy. Peak forces increased from approximately 1379 to approximately 2622 pN while an extended Hertz fit of force-indentation data showed a approximately 24 fold increase in Young's modulus on indentation. The effect of glutaraldehyde cross-linking on the tensile properties of a single collagen fibril was investigated by a novel methodology based on atomic force spectroscopy. The Young's modulus of a secluded fibril increased from approximately 407 MPa to approximately 1.1 GPa with glutaraldehyde treatment. Collectively, the findings indicate that cross-linking at the level of the collagen fibril is of key importance for the mechanical strength of tendon tissue. However, when comparing the effects at the level of the tendon fascicle and fibril, respectively, further questions are prompted regarding the pathways of force through the tendon microstructure as fibril strength seems to surpass that of the tendon fascicle.

AB - Conclusive insight into the microscopic principles that govern the strength of tendon and related connective tissues is lacking and the importance of collagen cross-linking has not been firmly established. The combined application of whole-tissue mechanical testing and atomic force spectroscopy allowed for a detailed characterization of the effect of cross-linking in rat-tail tendon. The cross-link inducing agent glutaraldehyde augmented the tensile strength of tendon fascicles. Stress at failure increased from approximately 8 MPa to approximately 39 MPa. The mechanical effects of glutaraldehyde at the tendon fibril level were examined by atomic force microscopy. Peak forces increased from approximately 1379 to approximately 2622 pN while an extended Hertz fit of force-indentation data showed a approximately 24 fold increase in Young's modulus on indentation. The effect of glutaraldehyde cross-linking on the tensile properties of a single collagen fibril was investigated by a novel methodology based on atomic force spectroscopy. The Young's modulus of a secluded fibril increased from approximately 407 MPa to approximately 1.1 GPa with glutaraldehyde treatment. Collectively, the findings indicate that cross-linking at the level of the collagen fibril is of key importance for the mechanical strength of tendon tissue. However, when comparing the effects at the level of the tendon fascicle and fibril, respectively, further questions are prompted regarding the pathways of force through the tendon microstructure as fibril strength seems to surpass that of the tendon fascicle.

KW - Animals

KW - Collagen

KW - Cross-Linking Reagents

KW - Glutaral

KW - Male

KW - Rats

KW - Rats, Wistar

KW - Spectrum Analysis

KW - Stress, Mechanical

KW - Tendons

KW - Tensile Strength

U2 - 10.1080/03008200802610040

DO - 10.1080/03008200802610040

M3 - Journal article

C2 - 19637057

VL - 50

SP - 211

EP - 222

JO - Connective Tissue Research

JF - Connective Tissue Research

SN - 0300-8207

IS - 4

ER -