| The collagens are a set of complex glycoproteins found in all multi-cellular animals. They possess an intrinsic ability to assemble into various supramolecular constructs—often fibrous in nature. The FLS-type is one such arrangement collagen forms in the presence of highly charged and flexible molecules such as AGP. In this work, AFM was utilized to study the following topics: The role of AGP and the effects of pH in the in-vitro FLS-type self-assembly process. The structure of typical and atypical FLS-type aggregates; including the performance of a nano-dissection on a single FLS-type fibril that exposed its internal anatomy for direct visualization, and the successful imaging of FLS-type fibrils in fluid. As well, the effects of solution conditions such as ionic strength and pH on FLS-type fibril stability were also studied. When appropriate, parallel native-type collagen results are also presented, primarily to contrast our findings for the FLS-type system. |
