Výsledky vyhledávání - "Timothy M. Pabst"

Role of configurational flexibility on the adsorption kinetics of bivalent bispecific antibodies on porous cation exchange resins

Autor: Timothy M. Pabst, Giorgio Carta, Lucas K. Kimerer, Alan K. Hunter

Publikováno v: Journal of chromatography. A. 1655

The adsorption kinetics of a monoclonal antibody (mAb) used as a reference and of bivalent bispecific antibodies (BiSAb) on a macroporous cation exchanger is studied experimentally by examining the transient patterns of bound protein within the parti

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::49b04da1eebd7fcf0dd032332a6209c9
https://pubmed.ncbi.nlm.nih.gov/34461348

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Chromatographic behavior of bivalent bispecific antibodies on cation exchange columns. I. Experimental observations and phenomenological model

Autor: Timothy M. Pabst, Giorgio Carta, Alan K. Hunter, Lucas K. Kimerer

Publikováno v: Journal of Chromatography A. 1601:121-132

The cation exchange chromatographic behavior of three homologous bivalent bispecific antibodies (BiSAb) is characterized for two different resins, Source 15S and ProPac WCX-10, having different base matrix, particle size, pore structure, and ligand c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2bb08027ae195f455240b34aef6d05c4
https://doi.org/10.1016/j.chroma.2019.04.012

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Chromatographic behavior of bivalent bispecific antibodies on cation exchange columns. II. Biomolecular perspectives

Autor: Giorgio Carta, Lucas K. Kimerer, Timothy M. Pabst, Alan K. Hunter

Publikováno v: Journal of Chromatography A. 1601:133-144

In Part I of this work we determined the experimental cation exchange behavior of bivalent bispecific antibodies (BiSAb) comprising a pair of single chain variable fragment (scFv) domains flexibly linked to a framework immunoglobulin G (IgG), which e

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::83c032ab4b786f81559f2c48cb8d87fb
https://doi.org/10.1016/j.chroma.2019.04.013

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Process optimization and protein engineering mitigated manufacturing challenges of a monoclonal antibody with liquid-liquid phase separation issue by disrupting inter-molecule electrostatic interactions

Autor: Haibin Luo, Timothy M. Pabst, William K. Wang, Qun Du, Melissa Damschroder, Alan K. Hunter

Publikováno v: mAbs. 11:789-802

We report a case study in which liquid-liquid phase separation (LLPS) negatively impacted the downstream manufacturability of a therapeutic mAb. Process parameter optimization partially mitigated the LLPS, but limitations remained for large-scale man

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a10d9704f0f99660ec120ecdd53e1bd7
https://doi.org/10.1080/19420862.2019.1599634

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Formation of transient highly-charged mAb clusters strengthens interactions with host cell proteins and results in poor clearance of host cell proteins by protein A chromatography

Autor: Haibin, Luo, Qun, Du, Chen, Qian, Michelle, Mlynarczyk, Timothy M, Pabst, Melissa, Damschroder, Alan K, Hunter, William K, Wang

Publikováno v: Journal of Chromatography A. 1679:463385

Protein A chromatography with a high salt wash usually leads to robust clearance of host cell proteins (HCPs) in most recombinant monoclonal antibodies (mAbs), but a small subset of recalcitrant mAbs show significant HCP copurification. In this study

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::13005e8f5dfcea50578c3ac790103d3a
https://doi.org/10.1016/j.chroma.2022.463385

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Safety risk management for low molecular weight process-related impurities in monoclonal antibody therapeutics: Categorization, risk assessment, testing strategy, and process development with leveraging clearance potential

Autor: Timothy M. Pabst, Haibin Luo, Sheau‐Chiann Wang, Guoling Xi, William K. Wang, David Robbins, Yuling Li, Chenghong Wei, Matthew Cox, Simone M. Nicholson

Publikováno v: Biotechnology Progress

Process‐related impurities (PRIs) derived from manufacturing process should be minimized in final drug product. ICH Q3A provides a regulatory road map for PRIs but excludes biologic drugs like monoclonal antibodies (mAbs) that contain biological PR

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f6e426af8e4ed6f816e04d8efb133cfa
https://pubmed.ncbi.nlm.nih.gov/33373106

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Author response for 'Safety Risk Management for Low Molecular Weight Process‐related Impurities in Monoclonal Antibody Therapeutics: Categorization, Risk Assessment, Testing Strategy, and Process Development With Leveraging Clearance Potential'

Autor: null Haibin Luo, null Yuling Li, null David Robbins, null Sheau‐Chiann Wang, null Guoling Xi, null Matthew Cox, null Simone M. Nicholson, null Chenghong Wei, null Timothy M. Pabst, null William K. Wang

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::bd41b36bca4080eb82991be419b93f6b
https://doi.org/10.1002/btpr.3119/v2/response1

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Chromatographic and adsorptive behavior of a bivalent bispecific antibody and associated fragments

Autor: Ben Niu, Weiguo Zhai, Timothy M. Pabst, Lucas K. Kimerer, Giorgio Carta, Alan K. Hunter

Publikováno v: Journal of Chromatography A. 1648:462181

The elution and adsorptive behavior of a bivalent bispecific antibody (BiSAb), comprising an IgG1 framework with a scFv domain genetically fused to each heavy chain C-terminus via flexible linkers, and of two associated fragments were studied on two

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fab6f2925a039483a67673581dec38e0
https://doi.org/10.1016/j.chroma.2021.462181

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Chromatographic behavior of bivalent bispecific antibodies on hydrophobic interaction chromatography columns

Autor: Timothy M. Pabst, Alan K. Hunter, Giorgio Carta, Lucas K. Kimerer

Publikováno v: Journal of Chromatography A. 1617:460836

The elution behavior of bivalent bispecific antibodies (BiSAb) comprising an immunoglobulin G framework genetically fused to a pair of single chain variable fragments (scFvs) was studied on hydrophobic interaction chromatography (HIC) columns using a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bbfe17f819933f9007e4433ef99136aa
https://doi.org/10.1016/j.chroma.2019.460836

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