Výsledky vyhledávání - "Thomas R. Slaney"

Enzymatic removal of sialic acid enables iCIEF stability monitoring of charge variants of a highly sialylated bispecific antibody

Autor: Björn‐Hendrik Peters, James Bautista, Thomas R. Slaney, Hongyue Guo, Richard Y.‐C. Huang, Mary E. Krause, Ming Zeng, Julie Cheng, Zhi Chen

Publikováno v: Electrophoresis6 References. 43(9-10)

Antibody-based therapeutic proteins have highly complex molecular structures. The final therapeutic protein product may contain a wide range of charge variants. Accurate analysis of this charge variant composition is critical to determine manufacturi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ecfb020ec0f8d0bb3513324f528272ca
https://pubmed.ncbi.nlm.nih.gov/35362108

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Unique Impacts of Methionine Oxidation, Tryptophan Oxidation, and Asparagine Deamidation on Antibody Stability and Aggregation

Autor: Magfur E. Alam, Thomas R. Slaney, Peter M. Tessier, Sambit R. Kar, Tapan K. Das, Anthony Leone, Lina Wu, Gregory V. Barnett

Publikováno v: Journal of Pharmaceutical Sciences. 109:656-669

Monoclonal antibodies are attractive therapeutic agents because of their impressive biological activities and favorable biophysical properties. Nevertheless, antibodies are susceptible to various types of chemical modifications, and the impact of suc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77c6fa5babbb0da9c5b4dbad6f8496b1
https://doi.org/10.1016/j.xphs.2019.10.051

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Enhancing Host-Cell Protein Detection in Protein Therapeutics Using HILIC Enrichment and Proteomic Analysis

Autor: Wei Wu, Qingyi Wang, Thomas R. Slaney, Li Tao, Richard Ludwig, Anthony Leone

Publikováno v: Analytical chemistry. 92(15)

Liquid chromatography-mass spectrometry (LC-MS)-based proteomics approaches have been widely used to identify residual host-cell proteins (HCPs) in support of process and product characterization for protein therapeutics. Particularly, these methods

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a42796dd85e4cbb2c1df2bce7eef8af3
https://pubmed.ncbi.nlm.nih.gov/32614163

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Codon-Directed Determination of the Biological Causes of Sequence Variants in Therapeutic Proteins

Autor: Gargi Gupta, Tapan K. Das, Wei Wu, Li Tao, Erik Langsdorf, Richard Ludwig, Thomas R. Slaney, Hangtian Song, Tao Jiang, Duncan McVey

Publikováno v: Analytical Chemistry. 89:12749-12755

Recombinant monoclonal antibodies (mAbs) manufactured from immortalized mammalian cell lines are becoming increasingly important as therapies. Ensuring the quality of expressed proteins is critical when developing manufacturing processes. Protein seq

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc2f4e672bebc21fdb50e2eaaa37d364
https://doi.org/10.1021/acs.analchem.7b02914

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Identification of a host cell protein impurity in therapeutic protein, P1

Autor: Girija Krishnamurthy, Sheetal Mehta, Lei Zhang, Harbhajan Dhillon, Hangtian Song, Heather Boux, Deepti Ahluwalia, Anulfo Valdez, Thomas R. Slaney

Publikováno v: Journal of Pharmaceutical and Biomedical Analysis. 141:32-38

Residual host cell proteins (HCPs) are process-related impurities present in biotherapeutics that can pose safety health risks to patients. An adequate control of HCP levels in the final product, and demonstration of HCP clearance throughout a produc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::659109dda6bd3b75dda6e869b63168b4
https://doi.org/10.1016/j.jpba.2017.03.065

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Deamidation Can Compromise Antibody Colloidal Stability and Enhance Aggregation in a pH-Dependent Manner

Autor: Tapan K. Das, Gregory V. Barnett, Charles G. Starr, Thomas R. Slaney, Peter M. Tessier, Magfur E. Alam

Publikováno v: Molecular pharmaceutics. 16(5)

Monoclonal antibodies must be both chemically and physically stable to be developed into safe and effective drugs. Although there has been considerable progress in separately understanding the molecular determinants of antibody chemical and physical

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ca914dadab981198da28d595f2cc2f2
https://pubmed.ncbi.nlm.nih.gov/30916563

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Probing the Tryptophan Environment in Therapeutic Proteins: Implications for Higher Order Structure on Tryptophan Oxidation

Autor: Tapan K. Das, Thomas R. Slaney, Yunping Huang, Sambit R. Kar, Anthony Leone, Gurusamy Balakrishnan, Li Tao, Gregory V. Barnett, Laurel Hoffman, Jacob Bongers, Naresh Chennamsetty

Publikováno v: Journal of pharmaceutical sciences. 108(6)

Tryptophan (Trp) oxidation in proteins leads to a number of events, including changes in color, higher order structure (HOS), and biological activity. We describe here a number of new findings through a comprehensive characterization of 6 monoclonal

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c34f0901eb516236eb163329999787c0
https://pubmed.ncbi.nlm.nih.gov/30639740

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