The Promise of Mutation Resistant Drugs for SARS-CoV-2 That Interdict in the Folding of the Spike Protein Receptor Binding Domain

Fernando Bergasa-Caceres, Herschel A. Rabitz

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

In recent work, we proposed that effective therapeutic drugs aimed at treating the SARS-CoV-2 infection could be developed based on interdicting in the early steps of the folding pathway of key viral proteins, including the receptor binding domain (RBD) of the spike protein. In order to provide for a drug target on the protein, the earliest contact-formation event along the dominant folding pathway of the RBD spike protein was predicted employing the Sequential Collapse Model (SCM). The segments involved in the predicted earliest contact were suggested to provide optimal folding interdiction target regions (FITRs) for potential therapeutic drugs, with a focus on folding interdicting peptides (FIPs). In this paper, we extend our analysis to include 13 known single mutations of the RBD spike protein as well as the triple mutation B1.351 and the recent double mutation B1.617.2. The results show that the location of the FITR does not change in any of the 15 studied mutations, providing for a mutation-resistant drug design strategy for the RBD-spike protein.

Original languageEnglish (US)
Pages (from-to)288-302
Number of pages15
JournalCOVID
Volume1
Issue number1
DOIs
StatePublished - Sep 2021

All Science Journal Classification (ASJC) codes

  • Immunology and Microbiology (miscellaneous)
  • Medicine (miscellaneous)
  • Infectious Diseases

Keywords

  • CoV
  • COVID
  • design
  • peptide
  • SARS
  • therapeutic

Fingerprint

Dive into the research topics of 'The Promise of Mutation Resistant Drugs for SARS-CoV-2 That Interdict in the Folding of the Spike Protein Receptor Binding Domain'. Together they form a unique fingerprint.

Cite this