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143. |
Structural polymorphism of collagen type I-heparin cofibrils
D. Stamov, K. Salchert, A. Springer, C. Werner, and T. Pompe
Soft Matter 5, 3461 (2009)
We report on the coexistence of 2 different supramolecular polymorphic forms of pepsin-digested collagen type I fibrils reconstituted in vitro in the presence of heparin. Detailed structural analysis using transmission electron microscopy and scanning force microscopy shows a hierarchy involving 3 different structural levels and banding patterns in the system: asymmetric segment longspacing (SLS) fibrils and symmetric segments with an average periodicity (AP) of 250-260 nm, symmetric fibrous longspacing (FLS IV) nanofibrils with AP of 165 nm, and cofibrils exhibiting an asymmetric D-periodicity of 67 nm with a striking resemblance to the native collagen type I banding pattern. The intercalation of the high negatively charged heparin in the fibrils is suggested as being the main trigger for the hierarchical formation of the polymorphic structures. We propose a model explaining the unexpected presence of a symmetric and asymmetric form in the system and the principles governing the symmetric or asymmetric fate of the molecules.
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last modified: 2018.04.11 Mi
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Prof. Dr. Gianaurelio Cuniberti
secretariat:
postal address:
Institute for Materials Science
TU Dresden
01062 Dresden, Germany
visitors and courier address:
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