ArticleComputational and structural biotechnology journal2021
Computationally-guided design and affinity improvement of a protein binder targeting a specific site on HER2.
Article in Computational and structural biotechnology journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Identification of Bruceine A as a novel HSP90AB1 inhibitor for suppressing hepatocellular carcinoma growth.Journal of advanced research · 2026Article
- SurfDiff: protein surface profiling for selective or broadly reactive epitope prioritisation in binder and immunogen design.bioRxiv : the preprint server for biology · 2025Article
- Surface plasmon resonance microscopy reveals N-glycosylation driven modulation of affinity and avidity of ErbB receptors in whole single pancreatic cancer cells.Glycobiology · 2025Article
- De Novo Design of High-Affinity HER2-Targeting Protein Minibinders.Biomolecules · 2025Article
- Applications of Artificial Intelligence in Biotech Drug Discovery and Product Development.MedComm · 2025Review
- Guiding Competitive Binding Assays Using Protein-Protein Interaction Prediction: The HER2-Affitin Use Case.ACS omega · 2024Article
- De novo design of alpha-beta repeat proteins.bioRxiv : the preprint server for biology · 2024Article
- Oligomeric states of ASC specks regulate inflammatory responses by inflammasome in the extracellular space.Cell death discovery · 2023Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A protein binder with a desired epitope and binding affinity is critical to the development of therapeutic agents. Here we present computationally-guided design and affinity improvement of a protein binder recognizing a specific site on domain IV of human epidermal growth factor receptor 2 (HER2). As a model, a protein scaffold composed of Leucine-rich repeat (LRR) modules was used. We designed protein binders which appear to bind a target site on domain IV using a computational method. Top 10 designs were expressed and tested with binding assays, and a lead with a low micro-molar binding affinity was selected. Binding affinity of the selected lead was further increased by two-orders of magnitude through mutual feedback between computational and experimental methods. The utility and potential of our approach was demonstrated by determining the binding interface of the developed protein binder through its crystal structure in complex with the HER2 domain IV.
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Registered trials
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