Thompson J I, Czernuszka J T
Department of Materials, University of Oxford, United Kingdom.
Biomed Mater Eng. 1995;5(1):37-48.
Samples of collagen were cross-linked by two different methods: (a) glutaraldehyde and (b) a combination of dehydrothermal treatment and cyanamide. The elastic modulus, the ultimate tensile strength (fracture stress), strain to failure, work of fracture, and fracture toughness were measured before and after cross-linking in ambient laboratory conditions, and during immersion in water. These tests were all performed over a range of strain rates. For collagen tested in the wet condition, it was found that cross-linking increased the elastic modulus from approximately 25-30 MPa, to between 55 and 60 MPa, but there was little effect on fracture stress, and strain to failure was reduced. The work of fracture of the collagen decreased on cross-linking. Cross-linking had the same effect on the elastic modulus, fracture stress, and strain to failure of dry collagen, but the work of fracture was unaffected. In conclusion, cross-linking increased the elastic modulus, reduced the strain to failure, and had little effect on the fracture stress of collagen under the present experimental conditions.
（a）戊二醛，以及（b）脱氢热处理与氰胺的组合。在环境实验室条件下以及浸泡于水中时，对交联前后的弹性模量、极限拉伸强度（断裂应力）、断裂应变、断裂功和断裂韧性进行了测量。所有这些测试均在一系列应变率下进行。对于在湿态下测试的胶原蛋白，发现交联使弹性模量从约25 - 30兆帕增加到55至60兆帕之间，但对断裂应力影响不大，且断裂应变降低。交联后胶原蛋白的断裂功降低。交联对干态胶原蛋白的弹性模量、断裂应力和断裂应变具有相同影响，但对断裂功无影响。总之，在当前实验条件下，交联增加了胶原蛋白的弹性模量，降低了断裂应变，且对其断裂应力影响不大。
