期刊
JOURNAL OF STRUCTURAL BIOLOGY
卷 170, 期 1, 页码 83-92出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jsb.2009.12.018
关键词
Extracellular matrix; Fibronectin; Elastin; Biomineralization; Hydroxyapatite
资金
- NSF-MRSEC Program [DMR0606387]
- Brookhaven National Laboratory-Stony Brook University Seed Grand Program
- NIH [R01 AR52379, R01 AR49286]
- USDOE [DE-ACO2-98CH10886]
The extracellular matrix (ECM) is composed of mixed protein fibers whose precise composition affects biomineralization. New methods are needed to probe the interactions of these proteins with calcium phosphate mineral and with each other. Here we follow calcium phosphate mineralization on protein fibers self-assembled in vitro from solutions of fibronectin, elastin and their mixture. We probe the surface morphology and mechanical properties of the protein fibers during the early stages. The development of mineral crystals on the protein matrices is also investigated. In physiological mineralization solution, the elastic modulus of the fibers in the fibronectin-elastin mixture increases to a greater extent than that of the fibers from either pure protein. In the presence of fibronectin, longer exposure in the mineral solution leads to the formation of amorphous calcium phosphate particles templated along the self-assembled fibers, while elastin fibers only collect calcium without any mineral observed during early stage. TEM images confirm that small needle-shape crystals are confined inside elastin fibers which suppress the release of mineral outside the fibers during late stage, while hydroxyapatite crystals form when fibronectin is present. These results demonstrate complementary actions of the two ECM proteins fibronectin and elastin to collect cations and template mineral, respectively. (C) 2009 Elsevier Inc. All rights reserved.
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