De novo selected hACE2 mimics that integrate hotspot peptides with aptameric scaffolds for binding tolerance of SARS-CoV-2 variantsopen access
- Authors
- Lee, M.; Kang, B.; Lee, J.; Lee, J.; Jung, S.T.; Son, C.Y.; Oh, S.S.
- Issue Date
- 2022
- Publisher
- American Association for the Advancement of Science
- Citation
- Science Advances, v.8, no.43
- Indexed
- SCIE
SCOPUS
- Journal Title
- Science Advances
- Volume
- 8
- Number
- 43
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/146993
- DOI
- 10.1126/sciadv.abq6207
- 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. © 2022 The Authors.
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Collections - Graduate School > Department of Biomedical Sciences > 1. Journal Articles
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