ABSTRACT
The frequent occurrence of viral variants is a critical problem in developing antiviral prophylaxis and therapy; along with stronger recognition of host cell receptors, the variants evade the immune system-based vaccines and neutralizing agents more easily. In this work, we focus on enhanced receptor binding of viral variants and demonstrate generation of receptor-mimicking synthetic reagents, capable of strongly interacting with viruses and their variants. The hotspot interaction of viruses with receptor-derived short peptides is maximized by aptamer-like scaffolds, the compact and stable architectures of which can be in vitro selected from a myriad of the hotspot peptide-coupled random nucleic acids. We successfully created the human angiotensin-converting enzyme 2 (hACE2) receptor-mimicking hybrid ligand that recruits the hACE2-derived receptor binding domain-interacting peptide to directly interact with a binding hotspot of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Experiencing affinity boosting by ~500% to Omicron, the de novo selected hACE2 mimic exhibited a great binding tolerance to all SARS-CoV-2 variants of concern.
Subject(s)
COVID-19 , Nucleic Acids , Humans , Angiotensin-Converting Enzyme 2/genetics , SARS-CoV-2/genetics , Spike Glycoprotein, Coronavirus/genetics , Spike Glycoprotein, Coronavirus/metabolism , Ligands , Receptors, Virus/metabolism , Peptidyl-Dipeptidase A/metabolism , Protein Binding , Peptides/metabolism , Antiviral AgentsABSTRACT
We developed a method for producing porous charged polymer nanosheets using frozen ice containing microplastics. Upon assessing SARS-CoV-2 filtration using nanosheets with 100 nm-sized pores, a high rejection rate of 96% was achieved. The charged surfaces of nanosheets further enabled the electrophoretic capture of the virus using a portable battery with additional real-time sensing capability.