Identification of structural stability of mutated Hepatitis B Virus capsid proteins by nanoenvironmental energetics measurements

Hepatitis B Virus (HBV) is a commonly occurring human pathogen with an estimated 300 million carriers worldwide. This work presents a bioinformatics approach toward identifying amino acids for point mutation in Hepatitis B capsid (HBc) protein to prevent interaction of the virion's core protein with its surface protein. Based on the nanoenvironmental energetic measurements using bioinformatics tools, point mutations in the dimeric region of core protein were studied for changes in the dimensions of the key geometric parameters. The results provide structural insight regarding the important parameters contributing to HBV synthesis. This work paves the way for future pharmaceutical applications aimed at destabilisation of the HBV capsid-surface protein interactions.