The major components of physiological bone, collagen type I and hydroxyapatite (HAp), work synergistically to enhance the osteoconductivity and regeneration properties [1]. The interface between collagen and HAp, is critical for bone’s remarkable functionality as a biological composite material [1]. The atomistic interactions between the two components and the mechanisms of biomineralization, however, are not conclusively understood. Elucidating atomic-scale interactions of collagen and HAp is critical to understanding the biology of bone formation, as well as developing novel therapeutic interventions in tissue regeneration [2,3]. Molecular Dynamics (MD) simulations were used to investigate model systems of tropocollagen, as well as their individual alpha-I and alpha-II collagen chains, to better understand the role of the triple-helical conformation in the interactions with HAp. The analysis of these systems extends to the influence of residue identity, peptide orientation, and HAp surface composition. The mechanisms could help future studies in the design of biomaterials to enhance and facilitate bone regeneration.
1. Stock SR. The Mineral-Collagen Interface in Bone. Calcif Tissue Int. 2015;97(3):262-80.
2. Alcântara ACS, Felix LC, Galvão DS, Sollero P, Skaf MS. Devising Bone Molecular Models at the Nanoscale: From Usual Mineralized Collagen Fibrils to the First Bone Fibers Including Hydroxyapatite in the Extra-Fibrillar Volume. Materials (Basel). 2022;15(6):2274.
3. Duanis-Assaf T, Hu T, Lavie M, Zhang Z, Reches M. Understanding the Adhesion Mechanism of Hydroxyapatite-Binding Peptide. Langmuir. 2022;38(3):968-978.
