Interlaboratory Comparison of Hydrogen-Deuterium Exchange Mass Spectrometry Measurements of the Fab fragment of NISTmAb

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Interlaboratory Comparison of Hydrogen-Deuterium Exchange Mass Spectrometry Measurements of the Fab fragment of NISTmAb. / Hudgens, Jeffrey W; Gallagher, Elyssia S; Karageorgos, Ioannis; Anderson, Kyle W; Filliben, James J; Huang, Richard Y-C; Chen, Guodong; Bou-Assaf, George M; Espada, Alfonso; Chalmers, Michael J; Harguindey, Eduardo; Zhang, Hui-Min; Walters, Benjamin T; Zhang, Jennifer; Venable, John D; Steckler, Caitlin; Park, Inhee; Brock, Ansgar; Lu, Xiaojun; Pandey, Ratnesh K; Chandramohan, Arun; Anand, Ganesh S; Nirudodhi, Sasidhar N; Sperry, Justin B; Rouse, Jason C; Carroll, James A; Rand, Kasper D; Leurs, Ulrike; Weis, David D; Al-Naqshabandi, Mohammed A; Hageman, Tyler S; Deredge, Daniel; Wintrode, Patrick L; Papanastasiou, Malvina; Lambris, John D; Li, Sheng; Urata, Sarah.

I: Analytical Chemistry, Bind 91, Nr. 11, 2019, s. 7336-7345.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Hudgens, JW, Gallagher, ES, Karageorgos, I, Anderson, KW, Filliben, JJ, Huang, RY-C, Chen, G, Bou-Assaf, GM, Espada, A, Chalmers, MJ, Harguindey, E, Zhang, H-M, Walters, BT, Zhang, J, Venable, JD, Steckler, C, Park, I, Brock, A, Lu, X, Pandey, RK, Chandramohan, A, Anand, GS, Nirudodhi, SN, Sperry, JB, Rouse, JC, Carroll, JA, Rand, KD, Leurs, U, Weis, DD, Al-Naqshabandi, MA, Hageman, TS, Deredge, D, Wintrode, PL, Papanastasiou, M, Lambris, JD, Li, S & Urata, S 2019, 'Interlaboratory Comparison of Hydrogen-Deuterium Exchange Mass Spectrometry Measurements of the Fab fragment of NISTmAb', Analytical Chemistry, bind 91, nr. 11, s. 7336-7345. https://doi.org/10.1021/acs.analchem.9b01100

APA

Hudgens, J. W., Gallagher, E. S., Karageorgos, I., Anderson, K. W., Filliben, J. J., Huang, R. Y-C., ... Urata, S. (2019). Interlaboratory Comparison of Hydrogen-Deuterium Exchange Mass Spectrometry Measurements of the Fab fragment of NISTmAb. Analytical Chemistry, 91(11), 7336-7345. https://doi.org/10.1021/acs.analchem.9b01100

Vancouver

Hudgens JW, Gallagher ES, Karageorgos I, Anderson KW, Filliben JJ, Huang RY-C o.a. Interlaboratory Comparison of Hydrogen-Deuterium Exchange Mass Spectrometry Measurements of the Fab fragment of NISTmAb. Analytical Chemistry. 2019;91(11):7336-7345. https://doi.org/10.1021/acs.analchem.9b01100

Author

Hudgens, Jeffrey W ; Gallagher, Elyssia S ; Karageorgos, Ioannis ; Anderson, Kyle W ; Filliben, James J ; Huang, Richard Y-C ; Chen, Guodong ; Bou-Assaf, George M ; Espada, Alfonso ; Chalmers, Michael J ; Harguindey, Eduardo ; Zhang, Hui-Min ; Walters, Benjamin T ; Zhang, Jennifer ; Venable, John D ; Steckler, Caitlin ; Park, Inhee ; Brock, Ansgar ; Lu, Xiaojun ; Pandey, Ratnesh K ; Chandramohan, Arun ; Anand, Ganesh S ; Nirudodhi, Sasidhar N ; Sperry, Justin B ; Rouse, Jason C ; Carroll, James A ; Rand, Kasper D ; Leurs, Ulrike ; Weis, David D ; Al-Naqshabandi, Mohammed A ; Hageman, Tyler S ; Deredge, Daniel ; Wintrode, Patrick L ; Papanastasiou, Malvina ; Lambris, John D ; Li, Sheng ; Urata, Sarah. / Interlaboratory Comparison of Hydrogen-Deuterium Exchange Mass Spectrometry Measurements of the Fab fragment of NISTmAb. I: Analytical Chemistry. 2019 ; Bind 91, Nr. 11. s. 7336-7345.

Bibtex

@article{681700fbde3a485d8fe7fe3921794d20,
title = "Interlaboratory Comparison of Hydrogen-Deuterium Exchange Mass Spectrometry Measurements of the Fab fragment of NISTmAb",
abstract = "Hydrogen-deuterium exchange mass spectrometry (HDX-MS) is an established, powerful tool for investigating protein-ligand interactions, protein folding, and protein dynamics. However, HDX-MS is still an emergent tool for quality control of biopharmaceuticals and for establishing dynamic similarity between a biosimilar and an innovator therapeutic. Because industry will conduct quality control and similarity measurements over a product lifetime and in multiple locations, an understanding of HDX-MS reproducibility is critical. To determine the reproducibility of continuous-labeling, bottom-up HDX-MS measurements, the present interlaboratory comparison project evaluated deuterium uptake data from the Fab fragment of NISTmAb reference material (PDB: 5K8A) from fifteen laboratories. Laboratories reported ≈ 89,800 centroid measurements for 430 proteolytic peptide sequences of the Fab fragment (≈ 78,900 centroids), giving ≈ 100 {\%} coverage, and ≈ 10,900 centroid measurements for 77 peptide sequences of the Fc fragment. Nearly half of peptide sequences are unique to the reporting laboratory, and only two sequences are reported by all laboratories. The majority of the laboratories (87 {\%}) exhibited centroid mass laboratory repeatability precisions of 〈 sLab 〉 ≤ (0.15 ± 0.01) Da (1σx ̅ ), and all laboratories achieved 〈 sLab 〉 ≤ 0.4 Da. For immersions of protein at THDX = (3.6 to 25) oC and for D2O exchange times of tHDX = (30 s to 4 h) the reproducibility of back-exchange corrected, deuterium uptake measurements for the 15 laboratories is σreproducibility15 Labs ( tHDX ) = (9.0 ± 0.9) {\%} (1σ). A 9 laboratory cohort that immersed samples at THDX = 25 oC exhibited reproducibility of σreproducibility25C cohort ( tHDX ) = (6.5 ± 0.6) {\%} for back-exchange corrected, deuterium uptake measurements.",
author = "Hudgens, {Jeffrey W} and Gallagher, {Elyssia S} and Ioannis Karageorgos and Anderson, {Kyle W} and Filliben, {James J} and Huang, {Richard Y-C} and Guodong Chen and Bou-Assaf, {George M} and Alfonso Espada and Chalmers, {Michael J} and Eduardo Harguindey and Hui-Min Zhang and Walters, {Benjamin T} and Jennifer Zhang and Venable, {John D} and Caitlin Steckler and Inhee Park and Ansgar Brock and Xiaojun Lu and Pandey, {Ratnesh K} and Arun Chandramohan and Anand, {Ganesh S} and Nirudodhi, {Sasidhar N} and Sperry, {Justin B} and Rouse, {Jason C} and Carroll, {James A} and Rand, {Kasper D} and Ulrike Leurs and Weis, {David D} and Al-Naqshabandi, {Mohammed A} and Hageman, {Tyler S} and Daniel Deredge and Wintrode, {Patrick L} and Malvina Papanastasiou and Lambris, {John D} and Sheng Li and Sarah Urata",
year = "2019",
doi = "10.1021/acs.analchem.9b01100",
language = "English",
volume = "91",
pages = "7336--7345",
journal = "Analytical Chemistry",
issn = "0003-2700",
publisher = "American Chemical Society",
number = "11",

}

RIS

TY - JOUR

T1 - Interlaboratory Comparison of Hydrogen-Deuterium Exchange Mass Spectrometry Measurements of the Fab fragment of NISTmAb

AU - Hudgens, Jeffrey W

AU - Gallagher, Elyssia S

AU - Karageorgos, Ioannis

AU - Anderson, Kyle W

AU - Filliben, James J

AU - Huang, Richard Y-C

AU - Chen, Guodong

AU - Bou-Assaf, George M

AU - Espada, Alfonso

AU - Chalmers, Michael J

AU - Harguindey, Eduardo

AU - Zhang, Hui-Min

AU - Walters, Benjamin T

AU - Zhang, Jennifer

AU - Venable, John D

AU - Steckler, Caitlin

AU - Park, Inhee

AU - Brock, Ansgar

AU - Lu, Xiaojun

AU - Pandey, Ratnesh K

AU - Chandramohan, Arun

AU - Anand, Ganesh S

AU - Nirudodhi, Sasidhar N

AU - Sperry, Justin B

AU - Rouse, Jason C

AU - Carroll, James A

AU - Rand, Kasper D

AU - Leurs, Ulrike

AU - Weis, David D

AU - Al-Naqshabandi, Mohammed A

AU - Hageman, Tyler S

AU - Deredge, Daniel

AU - Wintrode, Patrick L

AU - Papanastasiou, Malvina

AU - Lambris, John D

AU - Li, Sheng

AU - Urata, Sarah

PY - 2019

Y1 - 2019

N2 - Hydrogen-deuterium exchange mass spectrometry (HDX-MS) is an established, powerful tool for investigating protein-ligand interactions, protein folding, and protein dynamics. However, HDX-MS is still an emergent tool for quality control of biopharmaceuticals and for establishing dynamic similarity between a biosimilar and an innovator therapeutic. Because industry will conduct quality control and similarity measurements over a product lifetime and in multiple locations, an understanding of HDX-MS reproducibility is critical. To determine the reproducibility of continuous-labeling, bottom-up HDX-MS measurements, the present interlaboratory comparison project evaluated deuterium uptake data from the Fab fragment of NISTmAb reference material (PDB: 5K8A) from fifteen laboratories. Laboratories reported ≈ 89,800 centroid measurements for 430 proteolytic peptide sequences of the Fab fragment (≈ 78,900 centroids), giving ≈ 100 % coverage, and ≈ 10,900 centroid measurements for 77 peptide sequences of the Fc fragment. Nearly half of peptide sequences are unique to the reporting laboratory, and only two sequences are reported by all laboratories. The majority of the laboratories (87 %) exhibited centroid mass laboratory repeatability precisions of 〈 sLab 〉 ≤ (0.15 ± 0.01) Da (1σx ̅ ), and all laboratories achieved 〈 sLab 〉 ≤ 0.4 Da. For immersions of protein at THDX = (3.6 to 25) oC and for D2O exchange times of tHDX = (30 s to 4 h) the reproducibility of back-exchange corrected, deuterium uptake measurements for the 15 laboratories is σreproducibility15 Labs ( tHDX ) = (9.0 ± 0.9) % (1σ). A 9 laboratory cohort that immersed samples at THDX = 25 oC exhibited reproducibility of σreproducibility25C cohort ( tHDX ) = (6.5 ± 0.6) % for back-exchange corrected, deuterium uptake measurements.

AB - Hydrogen-deuterium exchange mass spectrometry (HDX-MS) is an established, powerful tool for investigating protein-ligand interactions, protein folding, and protein dynamics. However, HDX-MS is still an emergent tool for quality control of biopharmaceuticals and for establishing dynamic similarity between a biosimilar and an innovator therapeutic. Because industry will conduct quality control and similarity measurements over a product lifetime and in multiple locations, an understanding of HDX-MS reproducibility is critical. To determine the reproducibility of continuous-labeling, bottom-up HDX-MS measurements, the present interlaboratory comparison project evaluated deuterium uptake data from the Fab fragment of NISTmAb reference material (PDB: 5K8A) from fifteen laboratories. Laboratories reported ≈ 89,800 centroid measurements for 430 proteolytic peptide sequences of the Fab fragment (≈ 78,900 centroids), giving ≈ 100 % coverage, and ≈ 10,900 centroid measurements for 77 peptide sequences of the Fc fragment. Nearly half of peptide sequences are unique to the reporting laboratory, and only two sequences are reported by all laboratories. The majority of the laboratories (87 %) exhibited centroid mass laboratory repeatability precisions of 〈 sLab 〉 ≤ (0.15 ± 0.01) Da (1σx ̅ ), and all laboratories achieved 〈 sLab 〉 ≤ 0.4 Da. For immersions of protein at THDX = (3.6 to 25) oC and for D2O exchange times of tHDX = (30 s to 4 h) the reproducibility of back-exchange corrected, deuterium uptake measurements for the 15 laboratories is σreproducibility15 Labs ( tHDX ) = (9.0 ± 0.9) % (1σ). A 9 laboratory cohort that immersed samples at THDX = 25 oC exhibited reproducibility of σreproducibility25C cohort ( tHDX ) = (6.5 ± 0.6) % for back-exchange corrected, deuterium uptake measurements.

U2 - 10.1021/acs.analchem.9b01100

DO - 10.1021/acs.analchem.9b01100

M3 - Journal article

C2 - 31045344

VL - 91

SP - 7336

EP - 7345

JO - Analytical Chemistry

JF - Analytical Chemistry

SN - 0003-2700

IS - 11

ER -

ID: 217934034