In situ atomic force microscopy of partially demineralized human dentin collagen fibrils.

摘要: Dentin collagen fibrils were studied in situ by atomic force microscopy (AFM). New data on size distribution and the axial repeat distance of hydrated dehydrated type I are presented. Polished dentin disks from third molars partially demineralized with citric acid, leaving proteins matrix. At this stage not resolved AFM, but after exposure to NaOCl(aq) for 100-240 s, presumably due removal noncollagenous proteins, individual fibril network connected mineralized substrate revealed. High-aspect-ratio silicon tips tapping mode used image soft network. Hydrated showed three distinct groups diameters: 100, 91, 83 nm a narrow at 67 nm. Dehydration resulted broad diameters between 75 105 division into 67, 62, 57 Subfibrillar features (4 nm) observed fibrils. The gap depth thick thin repeating segments varied 3 7 Phase revealed mineral particles transition overlap zone This method appears be powerful tool analysis fibrillar structures calcified tissues may aid understanding differences affected chemical treatments or diseases.