Elastic energy storage in unmineralized and mineralized extracellular matrices (ECMs): A comparison between molecular modeling and experimental measurements

被引:29
作者
Freeman, JW [1 ]
Silver, FH [1 ]
机构
[1] Univ Med & Dent New Jersey, Robert Wood Johnson Med Sch, Dept Pathol & Lab Med, Piscataway, NJ 08854 USA
关键词
collagen; mineral; steric energy; elastic spring constant;
D O I
10.1016/j.jtbi.2004.04.018
中图分类号
Q [生物科学];
学科分类号
07 [理学]; 0710 [生物学]; 09 [农学];
摘要
In order to facilitate locomotion and limb movement many animals store energy elastically in their tendons. In the turkey, much of the force generated by the gastrocnemius muscle is stored as elastic energy during tendon deformation and not within the muscle. As limbs move, the tendons are strained causing the collagen fibers in the extracellular matrices to be strained. During growth, avian tendons mineralize in the portions distal to the muscle and show increased tensile strength, modulus, and energy stored per unit strain as a result. In this study the energy stored in unmineralized and mineralized collagen fibers was measured and compared to the amount of energy stored in molecular models. Elastic energy storage values calculated using the molecular model were slightly higher than those obtained from collagen fibers, but display the same increases in slope as the fiber data. We hypothesize that these increases in slope are due to a change from the stretching of flexible regions of the collagen molecule to the stretching of less flexible regions. The elastic modulus obtained from the unmineralized molecular model correlates well with elastic moduli of unmineralized collagen from other studies. This Study demonstrates the potential importance of molecular modeling in the design of new biomaterials. (C) 2004 Elsevier Ltd. All rights reserved.
引用
收藏
页码:371 / 381
页数:11
相关论文
共 37 条
[1]
ALEXANDER RM, 1984, AM ZOOL, V24, P85
[2]
Alexander RM, 1983, Animal mechanics
[3]
[Anonymous], 2012, Introduction to protein structure
[4]
Disrupted collagen architecture in the crystal structure of a triple-helical peptide with a Gly->Ala substitution [J].
Bella, J ;
Brodsky, B ;
Berman, HM .
CONNECTIVE TISSUE RESEARCH, 1996, 35 (1-4) :401-406
[5]
VARIATIONS IN COLLAGEN FIBRIL STRUCTURE IN TENDONS [J].
BRODSKY, B ;
EIKENBERRY, EF ;
BELBRUNO, KC ;
STERLING, K .
BIOPOLYMERS, 1982, 21 (05) :935-951
[6]
CHRISTIANSEN DL, 1993, CELL MATER, V3, P177
[7]
OPTIMIZATION OF EXTRUDED COLLAGEN-FIBERS FOR ACL RECONSTRUCTION [J].
DUNN, MG ;
AVASARALA, PN ;
ZAWADSKY, JP .
JOURNAL OF BIOMEDICAL MATERIALS RESEARCH, 1993, 27 (12) :1545-1552
[8]
FREEMAN JW, 2004, IN PRESS CONNECT TIS
[9]
Mechanical characterization of collagen fibers and scaffolds for tissue engineering [J].
Gentleman, E ;
Lay, AN ;
Dickerson, DA ;
Nauman, EA ;
Livesay, GA ;
Dee, KC .
BIOMATERIALS, 2003, 24 (21) :3805-3813
[10]
LOCALIZATION OF FLEXIBLE SITES IN THREAD-LIKE MOLECULES FROM ELECTRON-MICROGRAPHS - COMPARISON OF INTERSTITIAL, BASEMENT-MEMBRANE AND INTIMA COLLAGENS [J].
HOFMANN, H ;
VOSS, T ;
KUHN, K ;
ENGEL, J .
JOURNAL OF MOLECULAR BIOLOGY, 1984, 172 (03) :325-343