Molecular Interaction Analysis of SPARC–Collagen with Human Serum Albumin.

In this study, in-silico interaction analysis between Human serum albumin (HSA) and serum protein acidic and rich in cysteine (SPARC)–Collagen complex was performed to determine the binding affinity between the two proteins. Structure-based molecular interaction studies of the HSA–SPARC–Collagen complex were performed using ClusPro 2.0, ZDOCK and PatchDock servers. Molecular dynamics analysis was performed for the first-ranked complex structure (HSA–SPARC–Collagen complex) using GROMACS for a period of 125 nanoseconds to determine the stability of the complex. The results show higher structural interactive cumulative scores between the HSA and SPARC–Collagen complex. HSA–SPARC–Collagen complex predominantly has the Pi-alkyl and Pi-sigma interactions. The root mean square fluctuation (RMSF), root mean square deviation, solvent accessible surface area, radius of gyration and the number of hydrogen bonds show that formed complex is stable. In conclusion, our study provides an add-on for tuning drugs concerning albumin as a drug carrier by targeting the SPARC–Collagen complex for treating different ailments. Human serum albumin (HSA) bypasses the degradative lysozyme system and interacts with the SPARC-Collagen complex in the interstitium. Molecular docking and molecular dynamics studies between HSA and SPARC-Collagen complex have shown a greater affinity and stability. Tuning the drug molecules with the HSA and targeting SPARC-Collagen complex protein helps deliver the drugs in low doses to the tumor cells. [ABSTRACT FROM AUTHOR]