In-silico Analysis of Molecular Interaction Between Silk Proteins with BMP-2 Type IA and Type II Receptors

Abstract

Background: Alveolar ridge defects are commonly associated with delayed tooth replacement. Natural biomaterial with enhanced regenerative potential is always sought after as a primary choice for ridge reconstruction. Silk, a biopolymer with its constituent proteins (fibroin and sericin) has recently demonstrated promising outcomes in vitro. However, the molecular mechanism by which this occurs remains to be elucidated. Objective: We assessed the molecular interactions between silk proteins bone morphogenetic protein (BMP)-2 type IA and type II receptors using molecular docking. Methodology: The N-terminal domain of silk proteins and structural complex of BMP-2 type IA and type II receptors were considered for protein–protein docking using the high ambiguity-driven protein–protein docking (HADDOCK) server. HADDOCK scores are a measure of the predicted stability of the protein–protein complex, and a lower score indicates a more stable complex and a higher affinity for binding. Results: The HADDOCK scores and root mean square deviation value for interaction between silk proteins with BMP-2 type IA and type II receptors were (−114.2 ± 25.0 and −143.1 ± 11.3) and (2.9 ± 0.4 and 1.9 ± 0.5), respectively, for fibroin and (−1.8 ± 15.6 and −9.7 ± 25.2) and (3.5 ±0.3 and 0.9 ± 0.6), respectively, for sericin. Conclusion: The interaction between fibroin and BMP-2 receptors was more stable with higher affinity.