Peptides as Therapeutic Agents for Dengue Virus

Chew, Miaw-Fang; Poh, Keat-Seong; Poh, Chit-Laa

Previous studies have shown that the lateral loop located on E(III) played an important role in virus-host receptor(s) interaction [73, 131] , hence making it an interesting target. A short sequence (380-IGVEPGQLKL-389) in the lateral loop on the DENV-2 E(III) was used as a target to screen for potential antiviral peptides using the BioMoDroid algorithm [132] . Four different peptides were designed and DET4 (one of the peptides) was found to inhibit 85% DENV-2 at 500 µM. TEM images indicated that DET4 inhibited DENV-2 entry by causing structural abnormalities and alteration of the conformational changes of E proteins. On the contrary, Panya et al. (2014) targeted on the n-octyl-β-D-glycoside (βOG) hydrophobic pocket located in the domain I domain II interface of DV E protein [133] . A previous study has shown that the shift of two β-hairpins located at the hydrophobic pocket was essential to cause correct conformational changes during virus fusion step [113] . The importance of the βOG hydrophobic pocket was further validated as several compounds targeting this hydrophobic pocket were able to stop DENV infection [134, 135] . By using AUTODOCK v4.2 and CDOCKER DISCOVERY STUDIO v2.1 software, Panya et al. (2014) found a di-peptide, EF, to be the most effective antiviral peptide as it inhibited DENV-2 infection with the IC50 value of 96 µM [133] .