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Design Strategy to Create Antibody Mimetics Harbouring Immobilised Complementarity Determining Region Peptides for Practical Use

Kadonosono, Tetsuya ; Yimchuen, Wanaporn ; Ota, Yumi ; See, Kyra ; Furuta, Tadaomi ; Shiozawa, Tadashi ; Kitazawa, Maika ; Goto, Yu ; Patil, Akash ; Kuchimaru, Takahiro ; Kizaka-Kondoh, Shinae

Scientific reports, 2020-01, Vol.10 (1), p.891-891, Article 891 [Periódico revisado por pares]

England: Nature Publishing Group

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Título:
Design Strategy to Create Antibody Mimetics Harbouring Immobilised Complementarity Determining Region Peptides for Practical Use
Autor: Kadonosono, Tetsuya ; Yimchuen, Wanaporn ; Ota, Yumi ; See, Kyra ; Furuta, Tadaomi ; Shiozawa, Tadashi ; Kitazawa, Maika ; Goto, Yu ; Patil, Akash ; Kuchimaru, Takahiro ; Kizaka-Kondoh, Shinae
Assuntos: Antibodies, Monoclonal - immunology ; Antibodies, Monoclonal, Humanized - chemistry ; Antibodies, Monoclonal, Humanized - genetics ; Antibodies, Monoclonal, Humanized - metabolism ; Antigens - metabolism ; Breast cancer ; Cell Line, Tumor ; Complementarity ; Complementarity Determining Regions - genetics ; Complementarity Determining Regions - immunology ; Computer applications ; Drug Design ; Epitopes - metabolism ; ErbB-2 protein ; Fibroblast growth factor 2 ; HeLa Cells ; Humans ; Molecular Dynamics Simulation ; Monoclonal antibodies ; Peptides ; Protein Engineering - methods ; Proteins ; Receptor, ErbB-2 - genetics ; Receptor, ErbB-2 - immunology ; Receptor, ErbB-2 - metabolism ; Recombinant Proteins - genetics ; Recombinant Proteins - immunology ; Recombinant Proteins - metabolism ; Reproducibility of Results ; Stomach Neoplasms - immunology ; Stomach Neoplasms - metabolism ; Trastuzumab - chemistry ; Trastuzumab - genetics ; Trastuzumab - metabolism
É parte de: Scientific reports, 2020-01, Vol.10 (1), p.891-891, Article 891
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
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Descrição: 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 ) 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.
Editor: England: Nature Publishing Group
Idioma: Inglês

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Design Strategy to Create Antibody Mimetics Harbouring Immobilised Complementarity Determining Region Peptides for Practical Use

Kadonosono, Tetsuya ; Yimchuen, Wanaporn ; Ota, Yumi ; See, Kyra ; Furuta, Tadaomi ; Shiozawa, Tadashi ; Kitazawa, Maika ; Goto, Yu ; Patil, Akash ; Kuchimaru, Takahiro ; Kizaka-Kondoh, Shinae

England: Nature Publishing Group

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