Glutathione and thioredoxin systems contribute to recombinant monoclonal antibody interchain disulfide bond reduction during bioprocessing

2017 ◽  
Vol 114 (7) ◽  
pp. 1469-1477 ◽  
Author(s):  
Michael W. Handlogten ◽  
Min Zhu ◽  
Sanjeev Ahuja
Keyword(s):  
Monoclonal Antibody ◽  
Disulfide Bond ◽  
Recombinant Monoclonal Antibody ◽  
Interchain Disulfide Bond ◽  
Disulfide Bond Reduction

scholarly journals Untargeted proteomics reveals upregulation of stress response pathways during CHO-based monoclonal antibody manufacturing process leading to disulfide bond reduction

mAbs ◽  
2021 ◽  
Vol 13 (1) ◽  
pp. 1963094
Author(s):  
Seo-Young Park ◽  
Susan Egan ◽  
Anthony J. Cura ◽  
Kathryn L. Aron ◽  
Xuankuo Xu ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Stress Response ◽  
Disulfide Bond ◽  
Manufacturing Process ◽  
Disulfide Bond Reduction

Inhibition of botulinum neurotoxins interchain disulfide bond reduction prevents the peripheral neuroparalysis of botulism

2015 ◽  
Vol 98 (3) ◽  
pp. 522-530 ◽  
Author(s):  
Giulia Zanetti ◽  
Domenico Azarnia Tehran ◽  
Marcon Pirazzini ◽  
Thomas Binz ◽  
Clifford C. Shone ◽  
...  
Keyword(s):  
Disulfide Bond ◽  
Interchain Disulfide Bond ◽  
Botulinum Neurotoxins ◽  
Disulfide Bond Reduction

Glutamine deamidation of a recombinant monoclonal antibody

2008 ◽  
Vol 22 (24) ◽  
pp. 4081-4088 ◽  
Author(s):  
Hongcheng Liu ◽  
Georgeen Gaza-Bulseco ◽  
Chris Chumsae
Keyword(s):  
Monoclonal Antibody ◽  
Recombinant Monoclonal Antibody

When Good Intentions Go Awry: Modification of a Recombinant Monoclonal Antibody in Chemically Defined Cell Culture by Xylosone, an Oxidative Product of Ascorbic Acid

2015 ◽  
Vol 87 (15) ◽  
pp. 7529-7534 ◽  
Author(s):  
Chris Chumsae ◽  
Patrick Hossler ◽  
Haly Raharimampionona ◽  
Yu Zhou ◽  
Sean McDermott ◽  
...  
Keyword(s):  
Cell Culture ◽  
Monoclonal Antibody ◽  
Ascorbic Acid ◽  
Recombinant Monoclonal Antibody

scholarly journals Effects of an Interchain Disulfide Bond on Tropomyosin Structure: A Molecular Dynamics Study

2018 ◽  
Vol 19 (11) ◽  
pp. 3376 ◽  
Author(s):  
Natalia A. Koubassova ◽  
Sergey Y. Bershitsky ◽  
Andrey K. Tsaturyan
Keyword(s):  
Heart Failure ◽  
Molecular Dynamics ◽  
Disulfide Bond ◽  
Coiled Coil ◽  
Middle Part ◽  
Actin Binding ◽  
Cross Linking ◽  
Interchain Disulfide Bond ◽  
Structural And Functional Properties ◽  
The Cross

Tropomyosin (Tpm) is a coiled-coil actin-binding dimer protein that participates in the regulation of muscle contraction. Both Tpm chains contain Cys190 residues which are normally in the reduced state, but form an interchain disulfide bond in failing heart. Changes in structural and functional properties of Tpm and its complexes with actin upon disulfide cross-linking were studied using various experimental methods. To understand the molecular mechanism underlying these changes and to reveal the possible mechanism of the involvement of the cross-linking in heart failure, molecular dynamics (MD) simulations of the middle part of Tpm were performed in cross-linked and reduced states. The cross-linking increased bending stiffness of Tpm assessed from MD trajectories at 27 °C in agreement with previous experimental observations. However, at 40 °C, the cross-linking caused a decrease in Tpm stiffness and a significant reduction in the number of main chain hydrogen bonds in the vicinity of residues 133 and 134. These data are in line with observations showing enhanced thermal unfolding of the least stable part of Tpm at 30–40 °C and accelerated trypsin cleavage at residue 133 at 40 °C (but not at 27 °C) upon cross-linking. These results allow us to speculate about the possible mechanism of involvement of Tpm cross-linking to heart failure pathogenesis.

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