Ultrastructura studies on the collagen of the marine sponge Chondrosia reniformis nardo

被引:72
作者
Heinemann, Sascha
Ehrlich, Hermann
Douglas, Timothy
Heinemann, Christiane
Worch, Hartmut
Schatton, Wolfgang
Hanke, Thomas
机构
[1] Tech Univ Dresden, Max Bergmann Ctr Biomat, Inst Mat Sci, D-01069 Dresden, Germany
[2] KliniPharm, D-60318 Frankfurt, Germany
关键词
D O I
10.1021/bm700574y
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The ultrastructure of isolated fibrils of Chondrosia reniformis sponge collagen was investigated by collecting characteristic data, such as fibril thickness, width, D-band periodicity, and height modulation, using atomic force microscopy (AFM) and transmission electron microscopy (TEM). Therefore an adapted pre-processing of the insoluble collagen into homogeneous suspensions using neutral buffer solutions was essential, and several purification steps have been developed. Fourier transform infrared reflection -absorption spectroscopy (FT-IRAS) of the purified sponge collagen showed remarkable analogy of peak positions and intensities with the spectra of fibrillar calf skin type I collagen, despite the diverse phylogenetic and evolutionary origin. The sponge collagen's morphology is compared with that of other fibrillar collagens, and the typical banding of the separated single fibrils is discussed by comparison of topographical data obtained using AFM and corresponding TEM investigations using common staining methods. As the TEM images of the negatively stained fibrils showed alternating dark and light bands, AFM revealed a characteristic periodicity of protrusions (overlap zones) followed by two equal interband regions (gap zones). AFNI and TEM results were correlated and multiperiodicity in Chondrosia collagen's banding is demonstrated. The periodic dark bands observed in TEM images correspond directly to the periodic protrusions seen by AFNI. As a result, we provide an improved, updated model of the collagen's structure and organization.
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页码:3452 / 3457
页数:6
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