ArticleScientific reports2020
Design Strategy to Create Antibody Mimetics Harbouring Immobilised Complementarity Determining Region Peptides for Practical Use.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 24 citations in OpenAlex.
- In silico designing and optimization of anti-epidermal growth factor receptor scaffolds by complementary-determining regions-grafting technique.Quantitative biology (Beijing, China) · 2024Article
- Review
- Antibody-guided design and identification of CD25-binding small antibody mimetics using mammalian cell surface display.Scientific reports · 2021Article
- Extending traditional antibody therapies: Novel discoveries in immunotherapy and clinical applications.Molecular therapy oncolytics · 2021Review
- Strategic design to create HER2-targeting proteins with target-binding peptides immobilized on a fibronectin type III domain scaffold.RSC advances · 2020Article
- Mutational and biophysical robustness in a prestabilized monobody.The Journal of biological chemistryArticle
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Monoclonal antibodies (mAbs) are attractive therapeutics for treating a wide range of human disorders, and bind to the antigen through their complementarity-determining regions (CDRs). Small stable proteins containing structurally retained CDRs are promising alternatives to mAbs. In this report, we present a method to create such proteins, named fluctuation-regulated affinity proteins (FLAPs). Thirteen graft acceptor (GA) sites that efficiently immobilise the grafted peptide structure were initially selected from six small protein scaffolds by computational identification. Five CDR peptides extracted by binding energy calculations from mAbs against breast cancer marker human epithelial growth factor receptor type 2 (HER2) were then grafted to the selected scaffolds. The combination of five CDR peptides and 13 GA sites in six scaffolds revealed that three of the 65 combinations showed specific binding to HER2 with dissociation constants (K
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