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Many kinds of materials are currently used as artificial bone substitutes. Hydroxyapatite (HA), the same as the main inorganic component of bone, is one of commonly used bio-ceramics and has excellent bioactivity and biocompatibility with hard tissues. However, it has problems as the bone filler or bone tissue-engineering scaffold due to low fracture toughness and low degradation rate. Recently, biodegradable materials for bone tissue have been developed to respond the requirement. Collagen, the same as the main organic component of bone, is biocompatible, biodegradable and promotes cell adhesion. A composites associated with HA is expected to have early osteoconduction and bone replacement ability. The present study was to fabricate bone-like composites consist of HA and collagen. Besides the ossiferous ability of the material in vivo is evaluated by using rabbits. Bone-like composites were successfully fabricated in this study, associating the collagen with HA. And the composites presented good osteoconductive and bone replacement potential.

We have here an insight into the features of molecular structures of bio-polymers with α-helix structure using infrared spectrum and elucidated theoretically, its relationship with bio-functions. In this case, we analyzed first the features of molecular structure of collagen and collected further the infrared spectrum of absorption of collagen and bovine serum albumin containing α-helix conformation in 400–4000 cm^-1 as well as their changes of strength of infrared absorption with varying temperatures using Fourier Transform–Infrared (FT-IR) spectrometers in the region of 15–95°C. The results show that there is a new band of 1650 cm^-1 close to the amide-I band of 1666 cm^-1 or 1670 cm^-1 in these bio-polymers, its strength decreases exponentially with increasing temperature of the systems, which can be expressed by exp[-(0.437 + 8.987 × 10^-6 T²)], but 1666 cm^-1 band increases linearly with increasing temperature. We calculated the energy spectrum of the protein molecules with α-helix conformation using the Soliton Theory of bio-energy transport, which are basically same with the experimental results measured by us. From these results and soliton theory we can conclude that the nonlinear soliton excitation, corresponding to 1650 cm^-1 band and the exciton excitation, is related to 1666 cm^-1 band, exists in the collagen and bovine serum albumin. In the meanwhile, these results also verified that the soliton theory of bio-energy transport along α-helix bio-polymers is appropriate to the protein molecules with α-helix conformation. Therefore, the studied results are helpful to elucidate the relationship between the molecular structure and bio-function of these bio-polymers.

Collagen is the major component of the extracellular matrix in skin, tendon, cartilage, cornea, bone, etc., and as a main structural protein is the key determinant of mechanical and functional properties of tissues and organs. Proper balance between synthesis and degradation of collagen fibers is critical for maintaining normal physiologic function; therefore, the modification of collagen fibers in a controlled manner is of high importance for biomedicine. In this work, using second harmonic generation (SHG) and two-photon excited auto-fluorescence (TPEF) microscopy, we revealed that hypericin, a natural pigment extracted from plant, induced structural modification of collagen based tissues. Dynamics of the process was monitored by time-lapse multiphoton imaging. It was demonstrated that hypericin–mediated process was considerably irreversible and has a potential to be used for destroying of abnormal tissues and treatment of some diseases.