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Rabbit amelogenin fibrils (r-amf) and human amelogenin fibrils (h-amf) were fabricated to understand the structural characteristics of the amelogenin family. The fibrils were compared to amyloid fibrils that were formed from recombinant beta-amyloid (r-amyloid) peptide using an identical process for each peptide. The crystallographic structures of the peptides were virtually identical for each set of fibrils. Therefore, the significant variation in the fibrillar properties of the native peptides was not caused by a common fundamental sequence feature but rather appeared to be the result of structural diversity within the peptides themselves. Differences in the fibrillar properties of the peptides were analyzed using atomic force microscopy (AFM), and these differences resulted from the structural properties of the peptide chains. The mean thickness of r-amf and h-amf fibrils was estimated to be approximately 3.7 nm and approximately 2.0 nm, respectively. However, these values were significantly different from the mean thickness of r-amyloid fibrils (approximately 7.6 nm). Using a nonlinear elastic model, the fibrillar moduli for r-amf and h-amf were estimated to be approximately 14.6 and approximately 2.4 GPa, respectively. These values were equivalent to the fibrillar moduli of r-amyloid and were significantly greater than the modulus of r-amyloid. It is suggested that
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