- ePoster presentation
- Open Access
HbAHP-25, a peptide designed in silico, exhibits potent anti-HIV activity in vitro
BMC Infectious Diseases volume 14, Article number: E30 (2014)
Identifying and / or designing molecules that can inhibit HIV infection and be safe to the host cells is highly desired.
HbAHP-25 was designed in silico against CD4 binding domain of gp120 of HIV-1 by molecular docking using Z dock and PROSA softwares. ELISA and SPR were used to determine the binding ability of HbAHP-25 to gp120. Anti-HIV activity of this peptide was checked by two different assays, viz: a) On TZM bl cells, using luciferase assay; b) On CEM-GFP cells and PBMCs using p24 antigen assay. MTT assay, TER/microsphere assay and Immunofluorescence were used to determine the effect of HbAHP-25 on cell viability, epithelial monolayer integrity and permeability.
Five peptides were designed, and one of the peptides, HbAHP-25 , exhibits significant anti-HIV activity against various strains of HIV-1, such as HIV-1 Ada, HIV-1 NL4-3, and HIV-1 IIIB. ELISA and SPR revealed a direct interaction between HbAHP-25 and gp120, thereby inhibiting its interaction with CD4 receptor. The peptide didn’t affect cell viability even at higher concentrations; nor did it affect epithelial monolayer integrity or permeability. HbAHP-25 also did not interfere with any tight junction proteins such as ZO-1 and Clauddin-1, thus maintaining cell integrity as well.
The peptide has potent anti-HIV activity, and can be explored as a potential therapeutic /prophylactic/preventive agent.
About this article
Cite this article
Bashir, T., Kumar, C. & Reddy, K. HbAHP-25, a peptide designed in silico, exhibits potent anti-HIV activity in vitro. BMC Infect Dis 14 (Suppl 3), E30 (2014). https://doi.org/10.1186/1471-2334-14-S3-E30
- Tight Junction
- Molecular Docking
- Tight Junction Protein
- Affect Cell Viability