A novel mineralization-inductive peptide derived from CEMP1functinal domains.

A novel biomimetic peptide (P35) was designed and synthesized by combining the N-terminal 20 amino acids and the C-terminal 15 amino acids of cementum protein 1 (CEMP1), guided by molecular docking and plasmid-based molecular engineering (sequence: MGTSSTDSQQAGHRRCSTSNQGQGDTEDGRMTLMG). The peptide's role in biomineralization was investigated through in vitro mineralization assays of Type I collagen fibers and molecular dynamics simulations. In addition, we evaluated the ability of P35 to promote osteogenic and cementogenic differentiation in human periodontal ligament cells (hPDLCs). Our findings identified the N-terminal (N20) and C-terminal (C15) regions of CEMP1 as critical functional domains for regulating biomineralization. P35 exhibited superior binding affinity to both minerals and Type I collagen compared to individual N20 or C15 peptides, attributable to its enhanced structural flexibility and plasticity. Moreover, P35 significantly outperformed N20 and C15 in promoting osteogenic and cementogenic differentiation of hPDLCs. These results provide a strong theoretical basis for the potential clinical application of P35 in periodontal tissue and bone regeneration.