Production and Downstream Processing

Bergemann, Klaus; Eckermann, Christian; Garidel, Patrick; Grammatikos, Stefanos; Jacobi, Alexander; Kaufmann, Hitto; Kempken, Ralph; Pisch‐Heberle, Sandra

doi:10.1002/9783527619740.ch9

Cited by 29 publications

(15 citation statements)

References 55 publications

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“…The two mAbs were produced by mammalian cell culture technology using a CHO (Chinese hamster ovary) cell line. [3] [7] The isoelectric point of both IgG1s is ca. 8.4 with an average molecular weight of 150 kDa.…”

Section: Accepted Articlementioning

confidence: 99%

“…[2] These molecules are complex, so developing and producing them demands an interdisciplinary approach based on solid knowledge and a thorough understanding of mAb protein properties. [3] In particular, three amino acids have side chains with buffering potential in the pharmaceutically relevant range (pH 4.0 to pH 7.0): aspartate (pKa 3.7), glutamate (pKa 4.3), and histidine (pKa 6.5). As a result, mAbs (and other proteins that include these amino acids) can act as pH buffers themselves.…”

Section: Introductionmentioning

confidence: 99%

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Buffer‐free therapeutic antibody preparations provide a viable alternative to conventionally buffered solutions: From protein buffer capacity prediction to bioprocess applications

Bahrenburg

Karow

Garidel

2015

Biotechnology Journal

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Protein therapeutics, including monoclonal antibodies (mAbs), have significant buffering capacity, particularly at concentrations>50 mg/mL. This report addresses pH-related issues critical to adoption of self-buffered monoclonal antibody formulations. We evaluated solution conditions with protein concentrations ranging from 50 to 250 mg/mL. Samples were both buffer-free and conventionally buffered with citrate. Samples were non-isotonic or adjusted for isotonicity with NaCl or trehalose. Studies included accelerated temperature stability tests, shaking stability studies, and pH changes in infusion media as protein concentrate is added. We present averaged buffering slopes of capacity that can be applied to any mAb and present a general method for calculating buffering capacity of buffer-free, highly concentrated antibody liquid formulations. In temperature stability tests, neither buffer-free nor conventionally buffered solution conditions showed significant pH changes. Conventionally buffered solutions showed significantly higher opalescence than buffer-free ones. In general, buffer-free solution conditions showed less aggregation than conventionally buffered solutions. Shaking stability tests showed no differences between buffer-free and conventionally buffered solutions. "In-use" preparation experiments showed that pH in infusion bag medium can rapidly approximate that of self-buffered protein concentrate as concentrate is added. In summary, the buffer capacity of proteins can be predicted and buffer-free therapeutic antibody preparations provide a viable alternative to conventionally buffered solutions.

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Section: Accepted Articlementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Buffer‐free therapeutic antibody preparations provide a viable alternative to conventionally buffered solutions: From protein buffer capacity prediction to bioprocess applications

Bahrenburg

Karow

Garidel

2015

Biotechnology Journal

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“…Der Aufarbeitungsprozess muss dabei sowohl prozessbezogene als auch produktbezogene Verunreinigungen entfernen können. Zusätz-lich müssen auch potenziell eingetragene Viren abgereichert werden können [1,2]. Das API wird letztlich in eine lagerfähige Formulierung überführt und in geeignete Packmittel abgefüllt.…”

Section: Rentschler Biotechnologie Gmbh Laupheimunclassified

Die richtige Formulierung zum Erhalt der Qualität therapeutischer Proteine

Faude

Kohne

2011

Biospektrum

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“…Alors que quelques milligrammes suffisent pour des études au stade recherche, il n'est pas rare de produire plusieurs centaines de Kg du même anticorps destiné à certaines indications oncologiques (Figure 1). Au niveau des procédés de préparation des protéines recombinantes, on distingue généralement les plates-formes upstream et downstream, respectivement dédiées aux activités de culture cellulaire et de purification [21].…”

Section: De La Recherche à La Commercialisation : Changement D'échellunclassified

Du milligramme à la tonne d’anticorps monoclonaux

Cochet

Chartrain

2009

Med Sci (Paris)

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Production and Downstream Processing

Cited by 29 publications

References 55 publications

Buffer‐free therapeutic antibody preparations provide a viable alternative to conventionally buffered solutions: From protein buffer capacity prediction to bioprocess applications

Buffer‐free therapeutic antibody preparations provide a viable alternative to conventionally buffered solutions: From protein buffer capacity prediction to bioprocess applications

Die richtige Formulierung zum Erhalt der Qualität therapeutischer Proteine

Du milligramme à la tonne d’anticorps monoclonaux

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