Mechanical Properties of Collagen Fascicles From the Rabbit Patellar Tendon

[+] Author and Article Information
E. Yamamoto, K. Hayashi

Biomechanics Laboratory, Department of Mechanical Engineering, Faculty of Engineering Science, Osaka University, Osaka, 560, Japan

N. Yamamoto

Biomechanics Laboratory, Department of Mechanical Engineering, Faculty of Science and Engineering, Ritsumeikan University, Kusatsu, Shiga 525, Japan

J Biomech Eng 121(1), 124-131 (Feb 01, 1999) (8 pages) doi:10.1115/1.2798033 History: Received February 10, 1997; Revised August 09, 1998; Online October 30, 2007


Tensile and viscoelastic properties of collagen fascicles of approximately 300 μm in diameter, which were obtained from rabbit patellar tendons, were studied using a newly designed micro-tensile tester. Their cross-sectional areas were determined with a video dimension analyzer combined with a CCD camera and a low magnification microscope. There were no statistically significant differences in tensile properties among the fascicles obtained from six medial-to-lateral locations of the patellar tendon. Tangent modulus, tensile strength, and strain at failure of the fascicles determined at about 1.5 percent/s strain rate were 216 ± 68 MPa, 17.2 ± 4.1 MPa, and 10.9 ± 1.6 percent (mean ± S.D.), respectively. These properties were much different from those of bulk patellar tendons; for example, the tensile strength and strain at failure of these fascicles were 42 percent and 179 percent of those of bulk tendons, respectively. Tangent modulus and tensile strength of collagen fascicles determined at 1 percent/s strain rate were 35 percent larger than those at 0.01 percent/s. The strain at failure was independent of strain rate. Relaxation tests showed that the reduction of stress was approximately 25 percent at 300 seconds. These stress relaxation behavior and strain rate effects of collagen fascicles differed greatly from those of bulk tendons. The differences in tensile and viscoelastic properties between fascicles and bulk tendons may be attributable to ground substances, mechanical interaction between fascicles, and the difference of crimp structure of collagen fibrils.

Copyright © 1999 by The American Society of Mechanical Engineers
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