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- W2000834616 abstract "Bone tissue engineering seeks to develop viable substitutes that repair and maintain the function of human bone tissue. To fabricate a bone scaffold that mimics extracellular matrix, we have assembled hydroxyapatite (HAp) nanorods and HAp-binding fd bacteriophages selected from landscape phage libraries against HAp powder (biopanning). The phage peptides for the top six HAp-binding phages have been analyzed further with a computational biomolecular suite Rosetta to deduce high-resolution chemical interactions occurring at the peptide-HAp interface. To simulate the structural environment of coat proteins, we have adsorbed each peptide to HAp (100) monoclinic crystal while considering its helix tilt angle and c-terminus distance away from the mineral surface. The incorporation of geometrical constraints improves sampling of the predicted structures and scoring of the best binding coat peptide among the top six peptides. The predicted structure of the best binding peptide reveals possible key residues and local conformations that contribute to favorable HAp-phage interface energy, which is important in building a HAp nanorod scaffold for bone regeneration." @default.
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- W2000834616 date "2011-02-01" @default.
- W2000834616 modified "2023-09-30" @default.
- W2000834616 title "Fd Bacteriophage Coat Protein Structure Prediction and Design for the Assembly of Hydroxyapatite Nanorods and Bone Tissue Regeneration" @default.
- W2000834616 doi "https://doi.org/10.1016/j.bpj.2010.12.1077" @default.
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