@article {2513, title = {In-silico Analysis of Molecular Interaction Between Silk Proteins with BMP-2 Type IA and Type II Receptors}, journal = {Pharmacognosy Journal}, volume = {17}, year = {2025}, month = {June 2025}, pages = {378-383}, type = {Original Article}, chapter = {378}, 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{\textendash}protein docking using the high ambiguity-driven protein{\textendash}protein docking (HADDOCK) server. HADDOCK scores are a measure of the predicted stability of the protein{\textendash}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 {\textpm} 25.0 and -143.1 {\textpm} 11.3) and (2.9 {\textpm} 0.4 and 1.9 {\textpm} 0.5), respectively, for fibroin and (-1.8 {\textpm} 15.6 and -9.7 {\textpm} 25.2) and (3.5 {\textpm}0.3 and 0.9 {\textpm} 0.6), respectively, for sericin. Conclusion: The interaction between fibroin and BMP-2 receptors was more stable with higher affinity.

}, keywords = {biopolymer, Fibroin, HADDOCK, RMSD, Sericin}, doi = {10.5530/pj.2025.17.47}, author = {Nandhinee Thiagaraj and Lekha Ashokkumar and Ram Sabarish and Balaji SK} }