Modified MrNV viral capsids with GE11 peptide for binding colorectal cancer cells.

Virus‐like particles (VLPs) are useful nanoparticles with a great impact on medical nanotechnology. Macrobrachium rosenbergii nodavirus (MrNV), which causes white tail disease (WTD) in giant freshwater prawns, is an icosahedral virus and have 26–27 nm. Recombinant MrNV capsid proteins in Escherichia coli exhibit the self‐assembly of the attractive property of the nanocontainers. Therefore, we hypothesized that modified VLPs either by genetic modification on the C‐terminal domain should enhance specific targeting of VLPs to the destiny of cancer cells. This work thus aims to predict and test the exterior surface of MrNV capsids by genetic modification by the structural modeling and In vitro analysis. We engineered the GE11 peptide to replace the 349–360 residues of the MrNV protruding domain, to insert between the 354 and 355 residues of the MrNV protruding domain and to extend to the C‐terminal of the MrNV capsids, which presumably led the specific binding of modified VLPs to EGFR on cancer cells. However, the site for introducing GE11 peptide into protein still difficult to determine. Therefore, we use the computational method to submit algorithms Phyre2 and Swiss model for the structural prediction. All of the models modified MrNV‐VLPs with GE11 are purified and analyzed by SDS‐PAGE, western blot and TEM analysis. These results lead to an In vitro experiment to enhance binding into EGFR positive cancer cells. This research thus provides a fundamental insight of virus capsid structure and ultimately leads to the development of strategies in drug delivery for carrying therapeutic agents towards the specific host cells.