{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Iwamoto N"],"funding":["Takeda Science Foundation","Japan Agency for Medical Research and Development","Ministry of Education, Culture, Sports, Science and Technology","Astellas Foundation for Research on Metabolic Disorders","Tokyo Biochemical Research Foundation"],"pagination":["1596-1601"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10641909"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["14(11)"],"pubmed_abstract":["Mirror-image proteins (d-proteins) are promising scaffolds for drug discovery because of their high proteolytic stability and low immunogenic properties. Facile and reproducible processes for the preparation of functional d-proteins are required for their application in therapeutic biologics. In this study, we designed and synthesized a novel monobody variant with two cysteine substitutions that facilitate the synthetic process via sequential native chemical ligations and improve protein stability by disulfide bond formation. The synthetic anti-GFP monobody in this model study exhibited good binding affinity to the target enhanced green fluorescent protein. In vivo administration of the synthetic anti-GFP monobody (l-monobody) to mice induced antidrug antibody (ADA) production, whereas no "],"journal":["ACS medicinal chemistry letters"],"pubmed_title":["Design and Synthesis of Monobody Variants with Low Immunogenicity."],"pmcid":["PMC10641909"],"funding_grant_id":["JP20ak0101144","JP18H02555","JP22K19376","JP22H02747","JP20K21252","JP22KJ1842"],"pubmed_authors":["Iwamoto N","Oishi S","Nonaka M","Manabe A","Sato Y","Ohno H","Inuki S"],"additional_accession":[]},"is_claimable":false,"name":"Design and Synthesis of Monobody Variants with Low Immunogenicity.","description":"Mirror-image proteins (d-proteins) are promising scaffolds for drug discovery because of their high proteolytic stability and low immunogenic properties. Facile and reproducible processes for the preparation of functional d-proteins are required for their application in therapeutic biologics. In this study, we designed and synthesized a novel monobody variant with two cysteine substitutions that facilitate the synthetic process via sequential native chemical ligations and improve protein stability by disulfide bond formation. The synthetic anti-GFP monobody in this model study exhibited good binding affinity to the target enhanced green fluorescent protein. In vivo administration of the synthetic anti-GFP monobody (l-monobody) to mice induced antidrug antibody (ADA) production, whereas no ","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Nov","modification":"2025-04-04T09:36:58.89Z","creation":"2025-04-04T09:36:58.89Z"},"accession":"S-EPMC10641909","cross_references":{"pubmed":["37974939"],"doi":["10.1021/acsmedchemlett.3c00342"]}}