Camelid V H H affinity ligands enable separation of closely related biopharmaceuticals
Interest in new and diverse classes of molecules such as recombinant toxins, enzymes, and blood factors continues to grow for use a biotherapeutics. Compared to monoclonal antibodies, these novel drugs typically lack a commercially available affinity chromatography option, which leads to greater pro...
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Published in | Biotechnology journal Vol. 12; no. 2 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
Germany
01.02.2017
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Abstract | Interest in new and diverse classes of molecules such as recombinant toxins, enzymes, and blood factors continues to grow for use a biotherapeutics. Compared to monoclonal antibodies, these novel drugs typically lack a commercially available affinity chromatography option, which leads to greater process complexity, longer development timelines, and poor platformability. To date, for both monoclonal antibodies and novel molecules, affinity chromatography has been mostly reserved for separation of process-related impurities such as host cell proteins and DNA. Reports of affinity purification of closely related product variants and modified forms are much rarer. In this work we describe custom affinity chromatography development using camelid V
H antibody fragments as "tunable" immunoaffinity ligands for separation of product-related impurities. One example demonstrates high selectivity for a recombinant immunotoxin where no binding was observed for an undesired deamidated species. Also discussed is affinity purification of a coagulation factor through specific recognition of the gamma-carboxylglutamic acid domain. |
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AbstractList | Interest in new and diverse classes of molecules such as recombinant toxins, enzymes, and blood factors continues to grow for use a biotherapeutics. Compared to monoclonal antibodies, these novel drugs typically lack a commercially available affinity chromatography option, which leads to greater process complexity, longer development timelines, and poor platformability. To date, for both monoclonal antibodies and novel molecules, affinity chromatography has been mostly reserved for separation of process-related impurities such as host cell proteins and DNA. Reports of affinity purification of closely related product variants and modified forms are much rarer. In this work we describe custom affinity chromatography development using camelid V
H antibody fragments as "tunable" immunoaffinity ligands for separation of product-related impurities. One example demonstrates high selectivity for a recombinant immunotoxin where no binding was observed for an undesired deamidated species. Also discussed is affinity purification of a coagulation factor through specific recognition of the gamma-carboxylglutamic acid domain. |
Author | Pabst, Timothy M Hermans, Pim Wendeler, Michaela Hunter, Alan K Wang, Xiangyang Bezemer, Sandra |
Author_xml | – sequence: 1 givenname: Timothy M surname: Pabst fullname: Pabst, Timothy M organization: MedImmune, Department of Purification Process Sciences, Gaithersburg, MD, USA – sequence: 2 givenname: Michaela surname: Wendeler fullname: Wendeler, Michaela organization: MedImmune, Department of Purification Process Sciences, Gaithersburg, MD, USA – sequence: 3 givenname: Xiangyang surname: Wang fullname: Wang, Xiangyang organization: MedImmune, Department of Purification Process Sciences, Gaithersburg, MD, USA – sequence: 4 givenname: Sandra surname: Bezemer fullname: Bezemer, Sandra organization: Thermo Fisher Scientific, Naarden, The Netherlands – sequence: 5 givenname: Pim surname: Hermans fullname: Hermans, Pim organization: Thermo Fisher Scientific, Naarden, The Netherlands – sequence: 6 givenname: Alan K surname: Hunter fullname: Hunter, Alan K organization: MedImmune, Department of Purification Process Sciences, Gaithersburg, MD, USA |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/27677057$$D View this record in MEDLINE/PubMed |
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CitedBy_id | crossref_primary_10_1016_j_chroma_2024_464929 crossref_primary_10_1016_j_jbc_2023_104956 crossref_primary_10_1016_j_chroma_2022_463274 crossref_primary_10_1016_j_jbiosc_2022_06_002 crossref_primary_10_1016_j_seppur_2020_116693 crossref_primary_10_1016_j_seppur_2024_127009 crossref_primary_10_3389_fimmu_2017_00960 crossref_primary_10_1016_j_chroma_2022_463533 crossref_primary_10_3390_ijms24043354 crossref_primary_10_2139_ssrn_4184445 crossref_primary_10_1155_2020_3201630 |
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Keywords | Moxetumomab pasudotox Prothrombin Conformational epitopes Affinity chromatography VHH ligand |
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SubjectTerms | Antibodies - isolation & purification Bacterial Toxins - isolation & purification Chromatography, Affinity - methods Exotoxins - isolation & purification Prothrombin - isolation & purification |
Title | Camelid V H H affinity ligands enable separation of closely related biopharmaceuticals |
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