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 (KD) of 270-350 nM in biolayer interferometry and 24-65 nM in ELISA. The FLAPs specifically detected HER2-overexpressing cancer cells. Thus, the present strategy is a promising and practical method for developing small antibody mimetics.
journal_name
Sci Repjournal_title
Scientific reportsauthors
Kadonosono T,Yimchuen W,Ota Y,See K,Furuta T,Shiozawa T,Kitazawa M,Goto Y,Patil A,Kuchimaru T,Kizaka-Kondoh Sdoi
10.1038/s41598-020-57713-4subject
Has Abstractpub_date
2020-01-21 00:00:00pages
891issue
1issn
2045-2322pii
10.1038/s41598-020-57713-4journal_volume
10pub_type
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