Mapping the interactions of selective biochemical probes of antibody conformation by hydrogen-deuterium exchange mass spectrometry

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Standard

Mapping the interactions of selective biochemical probes of antibody conformation by hydrogen-deuterium exchange mass spectrometry. / Leurs, Ulrike; Beck, Hermann; Bonnington, Lea; Lindner, Ingo; Pol, Ewa; Rand, Kasper Dyrberg.

I: ChemBioChem, Bind 18, Nr. 11, 01.06.2017, s. 1016-1021.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Leurs, U, Beck, H, Bonnington, L, Lindner, I, Pol, E & Rand, KD 2017, 'Mapping the interactions of selective biochemical probes of antibody conformation by hydrogen-deuterium exchange mass spectrometry', ChemBioChem, bind 18, nr. 11, s. 1016-1021. https://doi.org/10.1002/cbic.201600670

APA

Leurs, U., Beck, H., Bonnington, L., Lindner, I., Pol, E., & Rand, K. D. (2017). Mapping the interactions of selective biochemical probes of antibody conformation by hydrogen-deuterium exchange mass spectrometry. ChemBioChem, 18(11), 1016-1021. https://doi.org/10.1002/cbic.201600670

Vancouver

Leurs U, Beck H, Bonnington L, Lindner I, Pol E, Rand KD. Mapping the interactions of selective biochemical probes of antibody conformation by hydrogen-deuterium exchange mass spectrometry. ChemBioChem. 2017 jun. 1;18(11):1016-1021. https://doi.org/10.1002/cbic.201600670

Author

Leurs, Ulrike ; Beck, Hermann ; Bonnington, Lea ; Lindner, Ingo ; Pol, Ewa ; Rand, Kasper Dyrberg. / Mapping the interactions of selective biochemical probes of antibody conformation by hydrogen-deuterium exchange mass spectrometry. I: ChemBioChem. 2017 ; Bind 18, Nr. 11. s. 1016-1021.

Bibtex

@article{3082ae3e1ff94cf680d6d3ba2fd41a4c,
title = "Mapping the interactions of selective biochemical probes of antibody conformation by hydrogen-deuterium exchange mass spectrometry",
abstract = "Protein-based pharmaceuticals represent the fastest growing group of drugs in development in the pharmaceutical industry. One of the major challenges in the discovery, development and distribution of biopharmaceuticals is the assessment of changes in their higher-order structure due to chemical modifications. Here, we investigate the interactions of three different biochemical probes (Fabs) generated to detect conformational changes in a therapeutic IgG1 antibody (mAbX) by local hydrogen-deuterium exchange mass spectrometry (HDX-MS). We show that two of the probes target the Fc part of the antibody, while the third probe binds to the hinge region. Through HDX-ETD, we can distinguish specific binding patterns of the Fc-binding probes on mAbX at the single amino acid level. Preliminary surface plasmon resonance (SPR) experiments show that these domain-selective Fab probes are sensitive to conformational changes in distinct regions of a full-length therapeutic antibody upon oxidation.",
keywords = "Journal Article",
author = "Ulrike Leurs and Hermann Beck and Lea Bonnington and Ingo Lindner and Ewa Pol and Rand, {Kasper Dyrberg}",
note = "{\textcopyright} 2017 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.",
year = "2017",
month = jun,
day = "1",
doi = "10.1002/cbic.201600670",
language = "English",
volume = "18",
pages = "1016--1021",
journal = "ChemBioChem",
issn = "1439-4227",
publisher = "Wiley - V C H Verlag GmbH & Co. KGaA",
number = "11",

}

RIS

TY - JOUR

T1 - Mapping the interactions of selective biochemical probes of antibody conformation by hydrogen-deuterium exchange mass spectrometry

AU - Leurs, Ulrike

AU - Beck, Hermann

AU - Bonnington, Lea

AU - Lindner, Ingo

AU - Pol, Ewa

AU - Rand, Kasper Dyrberg

N1 - © 2017 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

PY - 2017/6/1

Y1 - 2017/6/1

N2 - Protein-based pharmaceuticals represent the fastest growing group of drugs in development in the pharmaceutical industry. One of the major challenges in the discovery, development and distribution of biopharmaceuticals is the assessment of changes in their higher-order structure due to chemical modifications. Here, we investigate the interactions of three different biochemical probes (Fabs) generated to detect conformational changes in a therapeutic IgG1 antibody (mAbX) by local hydrogen-deuterium exchange mass spectrometry (HDX-MS). We show that two of the probes target the Fc part of the antibody, while the third probe binds to the hinge region. Through HDX-ETD, we can distinguish specific binding patterns of the Fc-binding probes on mAbX at the single amino acid level. Preliminary surface plasmon resonance (SPR) experiments show that these domain-selective Fab probes are sensitive to conformational changes in distinct regions of a full-length therapeutic antibody upon oxidation.

AB - Protein-based pharmaceuticals represent the fastest growing group of drugs in development in the pharmaceutical industry. One of the major challenges in the discovery, development and distribution of biopharmaceuticals is the assessment of changes in their higher-order structure due to chemical modifications. Here, we investigate the interactions of three different biochemical probes (Fabs) generated to detect conformational changes in a therapeutic IgG1 antibody (mAbX) by local hydrogen-deuterium exchange mass spectrometry (HDX-MS). We show that two of the probes target the Fc part of the antibody, while the third probe binds to the hinge region. Through HDX-ETD, we can distinguish specific binding patterns of the Fc-binding probes on mAbX at the single amino acid level. Preliminary surface plasmon resonance (SPR) experiments show that these domain-selective Fab probes are sensitive to conformational changes in distinct regions of a full-length therapeutic antibody upon oxidation.

KW - Journal Article

U2 - 10.1002/cbic.201600670

DO - 10.1002/cbic.201600670

M3 - Journal article

C2 - 28346764

VL - 18

SP - 1016

EP - 1021

JO - ChemBioChem

JF - ChemBioChem

SN - 1439-4227

IS - 11

ER -

ID: 177084155