ENHANCEMENT OF NS1 ANTIBODY RECOGNITION BY A B-Roll PEPTIDE STABILIZED WITH ECTOINE: IMPLICATIONS FOR DENGUE DIAGNOSTIC DEVELOPMENT

Abstrak

Dengue remains a major global health concern, and the development of accurate, affordable, and early diagnostic methods continues to be an urgent research priority. This study aimed to evaluate the antigenic properties of a peptide derived from the B-roll region of the dengue virus NS1 protein and to analyze its interaction with the anti-NS1 antibody. Enzyme-Linked Immunosorbent Assay (ELISA) results showed a significant, dose-dependent increase in OD450 values, indicating strong antigen–antibody recognition. The addition of ectoine enhanced this interaction, suggesting a synergistic role in maintaining the peptide’s structural stability and epitope presentation. Molecular dynamics (MD) simulations using AMBER 22 further revealed that the peptide binds stably within the Fab pocket of the anti-NS1 antibody (PDB ID: 7BSC), supported by persistent hydrogen bonding and minimal RMSD fluctuations over 500 ns.

These computational findings align with the experimental ELISA data, confirming the peptide antigenicity. Overall, the results demonstrate that the peptide possesses dual functionality as an NS1 inhibitor and as an antigenic epitope highlighting its potential application in developing peptide-based diagnostic assays for dengue virus detection.