Epitope-based chimeric peptide vaccine design against S, M and E proteins of SARS-CoV-2 etiologic agent of global pandemic COVID-19: an in silico approach

M. Shaminur Rahman; M. Nazmul Hoque; M. Rafiul Islam; Salma Akter; A. S. M. Rubayet-Ul-Alam; Mohammad Anwar Siddique; Otun Saha; Md. Mizanur Rahaman; Munawar Sultana; M. Anwar Hossain

The CoV-RMEN peptide was predicted to contain 43.2% alpha helix, 67.4% beta sheet, 303 and 12% turns (Fig. 6b, Supplementary Fig. 5 ) using CFSSP:Chou and Fasman secondary 304 structure prediction server. In addition, with regards to solvent accessibility of aa residues, 34% 305 were predicted to be exposed, 30% medium exposed, and 34% were predicted to be buried. Only 306 2 aa residues (0.0%) were predicted to be located in disordered domains by the RaptorX Property 307 server ( Supplementary Fig. 6 ). The Phyre2 server predicted the tertiary structure model of the 308 . CC-BY 4.0 International license author/funder. It is made available under a The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.03.30.015164 doi: bioRxiv preprint designed chimeric protein in 5 templates (c5x5bB, c2mm4A, c6vsbB, c5x29B and c6vybB) 309 based on heuristics to maximize confidence, percent identity and alignment coverage. The final 310 model of the CoV-RMEN peptide modelled at 82% with more than 90% confidence (Fig. 6c) . 311