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Modification of Ti6Al4V surfaces using collagen I, III, and fibronectin. I. Biochemical and morphological characteristics of the adsorbed matrix
Author(s) -
Bierbaum Susanne,
Beutner René,
Hanke Thomas,
Scharnweber Dieter,
Hempel Ute,
Worch Hartmut
Publication year - 2003
Publication title -
journal of biomedical materials research part a
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.849
H-Index - 150
eISSN - 1552-4965
pISSN - 1549-3296
DOI - 10.1002/jbm.a.10080
Subject(s) - fibrillogenesis , fibronectin , extracellular matrix , fibril , biophysics , materials science , collagen fibril , type i collagen , titanium , adsorption , morphology (biology) , collagen, type i, alpha 1 , ionic strength , nanotopography , matrix (chemical analysis) , biochemistry , chemistry , nanotechnology , composite material , biology , metallurgy , organic chemistry , genetics , endocrinology , aqueous solution
Studies in developmental and cell biology have established the fact that responses of cells are influenced to a large degree by morphology and composition of the extracellular matrix. Goal of this work is to use this basic principle to improve the biological acceptance of implants by modifying the surfaces with components of the extracellular matrix (ECM). Aiming at load‐bearing applications in bone contact, in this study the modification of titanium surfaces with the collagen types I and III in combination with fibronectin was undertaken; fibrillogenesis, fibril morphology and adsorption of type I, III and I/III‐cofibrils onto titanium were assessed. Increasing the collagen type III amount resulted in a decrease of fibril diameter, while no significant changes in adsorption could be detected. The amount of fibronectin bound to the heterotypic fibrils depended on fibrillogenesis parameters such as ionic strength or concentration of phosphate, and varied with the percentage of integrated type III collagen. © 2003 Wiley Periodicals, Inc. J Biomed Mater Res 67A: 421–430, 2003