X-ray diffraction study of in vitro calcification of tendon collagen.
Decalcified samples of turkey leg tendon were submitted to in vitro calcification in the presence of metastable solutions of calcium phosphate at different concentrations. The structural relationship between apatitic deposits and collagen fibrils was examined by high- and small-angle X-ray diffraction using conventional and synchrotron radiation sources. At high supersaturation the apatitic crystallites were deposited on the collagen fibrils with their crystallographic c-axis preferentially oriented parallel to the fibril axis. At lower supersaturation, a fraction of the apatitic crystallites also grew with the c-axis preferentially oriented parallel to the collagen fibril axis, whereas other exhibited a preferential orientation perpendicular to the fibril axis. The analysis of the small-angle X-ray diffraction data indicates that the deposition of the apatitic phase in the sample stored in solution at lower supersaturation induced modifications of the collagen electron density distribution in the axial direction, which can be attributed to the deposition of the inorganic crystallites inside the gap region of the collagen structure.
Bigi
A
A
Department of Chemistry G. Ciamician, University of Bologna, Italy.
Gandolfi
M
M
Koch
M H
MH
Roveri
N
N
D000818:Animals; D002113:Calcification, Physiologic; D002130:Calcium Phosphates / Q000737:chemistry / Q000494:pharmacology; D003094:Collagen / Q000032:analysis* / Q000378:metabolism; D003648:Decalcification Technique; D012996:Solutions; D013710:Tendons / Q000737:chemistry* / Q000378:metabolism; D014422:Turkeys
D002130:Calcium Phosphates; D012996:Solutions; C485828:alpha-tricalcium phosphate; C485830:tetracalcium phosphate; C485838:calcium phosphate, monobasic, anhydrous; D003094:Collagen; C020243:calcium phosphate; C485829:calcium phosphate, dibasic, anhydrous