Akademik Veri Yönetim Sistemi
Materials Today Communications, cilt.49, 2025 (SCI-Expanded, Scopus)
Our study systematically analyzes the molecular interactions between Bone Morphogenetic Protein-2 (BMP-2) receptor variants and one- and two-unit β-tricalcium phosphate (β-TCP) ligands at the atomic level, for the first time, in silico. One-unit (β-TCP1) and two-unit (β-TCP2) β-TCP ligands, modeled using the natural Whitlockite crystal template, were subjected to geometry optimization, and their binding affinities were calculated with four different BMP-2 receptor variants (PDB IDs: 1REW, 2H62, 3BMP, 4UI0). Molecular docking results showed that β-TCP2 complexes exhibit relatively higher electrostatic compatibility and enhanced binding affinity. The findings obtained from Density Functional Theory (DFT)-based quantum chemical analyses reveal the superiority of β-TCP2 in terms of facile polarization and enhanced chemical reactivity. The Highest Occupied Molecular Orbital (HOMO) and Lowest Unoccupied Molecular Orbital (LUMO) isosurface figures support the bifunctional binding mechanism of β-TCP structures by having electron donor and electron acceptor center molecules and ions. In our findings, the compatibility of the Fourier Transform Infrared (FTIR) analysis data of the 2H62/β-TCP1 and 2H62/β-TCP complexes with the literature findings confirms the validity of the computational model. In this context, our study aims to fill the gap in the literature regarding the molecular representation of protein–biomaterial interactions by comprehensively analyzing the interaction mechanisms of β-TCP ligands on BMP-2 receptors at the atomic level for the first time. In addition, our study aims to provide a scientific basis for the design of new biomaterials for bone regeneration by revealing the potential of β-TCP, a bioceramic, to act not only as a passive carrier but also as an active biomaterial that can directly interact with important bone proteins such as BMP-2.