Relevant bibliographies by topics / Biopharmaceutical proteins

Academic literature on the topic 'Biopharmaceutical proteins'

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Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Biopharmaceutical proteins"

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Liu, Shulei, and Benjamin L. Schulz. "Biopharmaceutical quality control with mass spectrometry." Bioanalysis 13, no. 16 (August 2021): 1275–91. http://dx.doi.org/10.4155/bio-2021-0123.

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Mass spectrometry (MS) is a powerful technique for protein identification, quantification and characterization that is widely applied in biochemical studies, and which can provide data on the quantity, structural integrity and post-translational modifications of proteins. It is therefore a versatile and widely used analytic tool for quality control of biopharmaceuticals, especially in quantifying host-cell protein impurities, identifying post-translation modifications and structural characterization of biopharmaceutical proteins. Here, we summarize recent advances in MS-based analyses of these key quality attributes of the biopharmaceutical development and manufacturing processes.
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Todorovic, Zoran, and Dragana Protic. "Bioethical issues in the development of biopharmaceuticals." Filozofija i drustvo 23, no. 4 (2012): 49–56. http://dx.doi.org/10.2298/fid1204049t.

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Development of biopharmaceuticals is a challenging issue in bioethics. Unlike conventional, small molecular weight drugs, biopharmaceuticals are proteins derived from DNA technology and hybrid techniques with complex three dimensional structures. Immunogenicity of biopharmaceuticals should always be tested in clinical settings due to low predictive value of preclinical animal models. However, non-human primates (NHP) and transgenic mice could be used to address certain aspects of immunogenicity. Substantial efforts have been made to reduce NHP use in biopharmaceutical drug development, e.g. study design improvements and changes in regulatory policy. In addition, several expert groups are active in this field (e.g. NC3Rs, BioSafe, and Biopharmaceutical Technical Group). Despite that, there is an increasing trend of use of NHP in preclinical safety testing of biopharmaceuticals, especially regarding monoclonal antibodies. Other potential bioethical issues related biopharmaceutical drug development are their cost/effectiveness ratio, clinical safety assessment, production of biosimilars, and comparison of their efficacy with placebo in countries without intention to market. Identification of the human genome has opened many new bioethical issues. Development of biopharmaceuticals is an important bioethical issue for several reasons. It connects all aspects of contemporary bioethics: bio?medicine (e.g. clinical trials in vulnerable subjects), animal welfare and the most recent ad?vances in biotechnology. In particular, biopharmaceutical drug development is a challenging issue regarding treatment of rare diseases.
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Barolo, Lorenzo, Raffaela M. Abbriano, Audrey S. Commault, Jestin George, Tim Kahlke, Michele Fabris, Matthew P. Padula, Angelo Lopez, Peter J. Ralph, and Mathieu Pernice. "Perspectives for Glyco-Engineering of Recombinant Biopharmaceuticals from Microalgae." Cells 9, no. 3 (March 5, 2020): 633. http://dx.doi.org/10.3390/cells9030633.

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Microalgae exhibit great potential for recombinant therapeutic protein production, due to lower production costs, immunity to human pathogens, and advanced genetic toolkits. However, a fundamental aspect to consider for recombinant biopharmaceutical production is the presence of correct post-translational modifications. Multiple recent studies focusing on glycosylation in microalgae have revealed unique species-specific patterns absent in humans. Glycosylation is particularly important for protein function and is directly responsible for recombinant biopharmaceutical immunogenicity. Therefore, it is necessary to fully characterise this key feature in microalgae before these organisms can be established as industrially relevant microbial biofactories. Here, we review the work done to date on production of recombinant biopharmaceuticals in microalgae, experimental and computational evidence for N- and O-glycosylation in diverse microalgal groups, established approaches for glyco-engineering, and perspectives for their application in microalgal systems. The insights from this review may be applied to future glyco-engineering attempts to humanize recombinant therapeutic proteins and to potentially obtain cheaper, fully functional biopharmaceuticals from microalgae.
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Zhang, Fangrong, Gesa Richter, Benjamin Bourgeois, Emil Spreitzer, Armin Moser, Andreas Keilbach, Petra Kotnik, and Tobias Madl. "A General Small-Angle X-ray Scattering-Based Screening Protocol for Studying Physical Stability of Protein Formulations." Pharmaceutics 14, no. 1 (December 28, 2021): 69. http://dx.doi.org/10.3390/pharmaceutics14010069.

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A fundamental step in developing a protein drug is the selection of a stable storage formulation that ensures efficacy of the drug and inhibits physiochemical degradation or aggregation. Here, we designed and evaluated a general workflow for screening of protein formulations based on small-angle X-ray scattering (SAXS). Our SAXS pipeline combines automated sample handling, temperature control, and fast data analysis and provides protein particle interaction information. SAXS, together with different methods including turbidity analysis, dynamic light scattering (DLS), and SDS-PAGE measurements, were used to obtain different parameters to provide high throughput screenings. Using a set of model proteins and biopharmaceuticals, we show that SAXS is complementary to dynamic light scattering (DLS), which is widely used in biopharmaceutical research and industry. We found that, compared to DLS, SAXS can provide a more sensitive measure for protein particle interactions, such as protein aggregation and repulsion. Moreover, we show that SAXS is compatible with a broader range of buffers, excipients, and protein concentrations and that in situ SAXS provides a sensitive measure for long-term protein stability. This workflow can enable future high-throughput analysis of proteins and biopharmaceuticals and can be integrated with well-established complementary physicochemical analysis pipelines in (biopharmaceutical) research and industry.
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Nielsen, Jens. "Production of biopharmaceutical proteins by yeast." Bioengineered 4, no. 4 (July 2013): 207–11. http://dx.doi.org/10.4161/bioe.22856.

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Webber, Matthew J., Eric A. Appel, Brittany Vinciguerra, Abel B. Cortinas, Lavanya S. Thapa, Siddharth Jhunjhunwala, Lyle Isaacs, Robert Langer, and Daniel G. Anderson. "Supramolecular PEGylation of biopharmaceuticals." Proceedings of the National Academy of Sciences 113, no. 50 (November 28, 2016): 14189–94. http://dx.doi.org/10.1073/pnas.1616639113.

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The covalent modification of therapeutic biomolecules has been broadly explored, leading to a number of clinically approved modified protein drugs. These modifications are typically intended to address challenges arising in biopharmaceutical practice by promoting improved stability and shelf life of therapeutic proteins in formulation, or modifying pharmacokinetics in the body. Toward these objectives, covalent modification with poly(ethylene glycol) (PEG) has been a common direction. Here, a platform approach to biopharmaceutical modification is described that relies on noncovalent, supramolecular host–guest interactions to endow proteins with prosthetic functionality. Specifically, a series of cucurbit[7]uril (CB[7])–PEG conjugates are shown to substantially increase the stability of three distinct protein drugs in formulation. Leveraging the known and high-affinity interaction between CB[7] and an N-terminal aromatic residue on one specific protein drug, insulin, further results in altering of its pharmacological properties in vivo by extending activity in a manner dependent on molecular weight of the attached PEG chain. Supramolecular modification of therapeutic proteins affords a noncovalent route to modify its properties, improving protein stability and activity as a formulation excipient. Furthermore, this offers a modular approach to append functionality to biopharmaceuticals by noncovalent modification with other molecules or polymers, for applications in formulation or therapy.
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Owczarek, B., A. Gerszberg, and K. Hnatuszko-Konka. "A Brief Reminder of Systems of Production and Chromatography-Based Recovery of Recombinant Protein Biopharmaceuticals." BioMed Research International 2019 (January 8, 2019): 1–13. http://dx.doi.org/10.1155/2019/4216060.

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Recombinant proteins are produced for various applications in laboratory and industrial settings. Among them, therapeutic applications have evolved into a mature field in recent years, affecting the face of contemporary medical treatment. This, in turn, has stimulated an ever-greater need for innovative technologies for the description, expression, and purification of recombinant protein biopharmaceuticals. Therefore, many biopharmaceuticals are synthesized in heterologous systems to obtain satisfactory yields that cannot be provided by natural sources. As more than 35 years has passed since the first recombinant biopharmaceutical (human insulin) successfully completed clinical trials in humans, we provide a brief review of the available prokaryotic and eukaryotic expression systems, listing the advantages and disadvantages of their use. Some examples of therapeutic proteins expressed in heterologous hosts are also provided. Moreover, technologies for the universal extraction of protein molecules are mentioned here, as is the methodology of their purification.
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Buyel, Johannes Felix, and Rainer Fischer. "Downstream processing of biopharmaceutical proteins produced in plants." Bioengineered 5, no. 2 (February 3, 2014): 138–42. http://dx.doi.org/10.4161/bioe.28061.

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Howard, John A. "Commercialization of Biopharmaceutical and Bioindustrial Proteins from Plants." Crop Science 45, no. 2 (March 2005): 468–72. http://dx.doi.org/10.2135/cropsci2005.0468.

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Creamer, Jessica S., Nathan J. Oborny, and Susan M. Lunte. "Recent advances in the analysis of therapeutic proteins by capillary and microchip electrophoresis." Anal. Methods 6, no. 15 (2014): 5427–49. http://dx.doi.org/10.1039/c4ay00447g.

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Dissertations / Theses on the topic "Biopharmaceutical proteins"

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Wei, Tzu-Hsiang Biotechnology &amp Biomolecular Sciences Faculty of Science UNSW. "Transient production of biopharmaceutical proteins." Publisher:University of New South Wales. Biotechnology & Biomolecular Sciences, 2009. http://handle.unsw.edu.au/1959.4/43708.

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The creation of stable mammalian cell lines for biopharmaceutical production often require several months, and is unfavourable for the rapid production of multiple drug candidates for screening in the early stages of development. Biopharmaceutical production by transient transfection provides a possible alternative of quickly producing these early stage drug candidates. The Epi-CHO transient expression system, which consists of a Chinese hamster ovary (CHO) cell line (CHO-T) expressing the murine polyomavirus Large T-Antigen (LT), emonstrated enhanced transient recombinant protein production. The aim of this study was to prolong transient recombinant protein prod.Jction of the Epi-CHO expression system by creating a CHO cell line expressing both LT and EBNA1 (ECHO-T). The pEBNA1-LT expression vector encoding LT and EBNA1 was constructed and transfected into CHO-K1. A total of 20 clones were isolated from the antibioticresistant pool and screened for the expression of functional LT and EBNA1. PCR analysis showed 16 of the 20 clones was positive for EBNA1 and LT DNA. Of the 16 clones, six were positive for EBNA1 and LT expression by RT-PCR. Detection of LT and EBNA1 by immunofluorescence showed positive staining for the P7-G3 clone. Western blotting suggested the P7-G3 clone was: positive for EBNA1, and clones P3-C7 and P7-E2 were positive for LT. A plasmid replication assay confirmed the expression of functional LT in all six clones. Plasmid maintenance assay confirmed clone P7-G3 as the ECHO-T clones to express functional EBNA1. The P7-G3 clone demonstrated prolonged and sustained transient recombinant protein expression when compared to CHO-T. The P7-G3 clone achieved sustained transient protein expression for 32 days in the absence of selection, the longest currently reported for CHO cells.
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Pradhan, S. "Rational design of enterokinase for the development of enhanced biopharmaceutical proteins." Thesis, University College London (University of London), 2013. http://discovery.ucl.ac.uk/1378549/.

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Enterokinase (EK) is a serine protease used to cleave therapeutic recombinant proteins during downstream processing. It has been selected for the activation and cleavage of a range of proprietary fusion proteins developed by Syntaxin Ltd. Whilst EK is well suited to this role in regards to substrate specificity, it has drawbacks, especially when it comes to expression in bacterial cells. Expression of EK in bacterial cells is the preferred expression method for process optimisation but is problematic due to its preference for inclusion body formation. This project describes efforts for improving the solubility of EK in E. coli using different constructs and mutagenesis. A total of four constructs were tested with two found to be soluble and one partially soluble. Two of the constructs (D4K-EK & pelB-EK) were found to readily form inclusion bodies (IB). Refolding of these constructs was undertaken and optimised using DoE. Only the refolded pelB EK showed significant activity, but refolded activity was found to vary greatly based on IB quality. The partially soluble pelB-EK construct exports to the periplasm for activation and soluble expression and was chosen for mutagenesis studies to improve soluble expression. A rational design approach using a range of sequence and structural bioinformatics methods including the consensus sequence, Hotpatch and statistical coupling analysis were utilised to identify fifteen stabilising mutants and seven mutants designed to increase surface charge. Of these potential mutants, ten (five stabilising, five surface charge) were created and analysed for activity, soluble yield and changes to secondary structure. Seven of the ten mutants showed measurable activity. Of interest were the surface charge mutants, which helped improve the purified yield by up to 2.5 fold. Also of note was consensus mutant V30Q which helped improve activity of periplasmic EK by 4.3 fold, whilst A32S and A44G visibly improved the thermo-tolerance of EK.
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Batra, Sumit. "Innovative Purification Protocol for Heparin Binding Proteins: Relevance in Biopharmaceutical and Biomedical Applications." TopSCHOLAR®, 2011. http://digitalcommons.wku.edu/theses/1062.

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Heparin binding (HB) proteins mediates a wide range of important cellular processes, which makes this class of proteins biopharmaceutically important. Engineering HB proteins could bring many advantages, but it necessitates cost effective and efficient purification methodologies compared to the currently available methods. One of the most important classes of heparin binding protein is the fibroblast growth factors (FGFs) and its receptors (FGFRs). In this study, we report an efficient off-column purification of FGF-1 from soluble fractions and purification of the D2 domain of FGFR from insoluble inclusion bodies, using a weak amberlite cation (IRC) exchanger. This approach is an alternative to conventional affinity column chromatography, which exhibit several disadvantages, including time-consuming experimental procedures and regeneration and results in high cost for production of recombinant proteins. Authenticity of the purified proteins was verified by SDS-PAGE and MALDI mass spectrum analysis. Results of the heparin binding chromatography and steady state fluorescence experiments showed that the FGF-1 and the D2 are in a native biologically active conformation. The findings of this study will not only aid an in-depth investigation of this class of proteins but will also provide avenues for inexpensive and efficient purification of other important biological macromolecules.
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Buyel, Johannes Felix [Verfasser]. "Manufacturing biopharmaceutical proteins by transient expression in Nicotiana tabacum (L.) / Johannes Felix Buyel." Aachen : Hochschulbibliothek der Rheinisch-Westfälischen Technischen Hochschule Aachen, 2013. http://d-nb.info/1043518819/34.

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Hameed, Rana Majeed. "The application of aqueous two phase systems to the analysis of protein isoforms of importance in clinical biochemistry and biopharmaceutical production." Thesis, Brunel University, 2016. http://bura.brunel.ac.uk/handle/2438/14452.

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Aqueous Phase Partitioning has a long history of applications to the analytical characterisation of biomolecules. However process applications have attracted the most interest in biotechnology where it has become widely recognized as a cost-effective technique. The main aim of this work was to explore the proposition that partition in Aqueous Two Phase Systems (ATPS) can be used as an analytical tool to detect protein isoforms and to assess the applicability of the method in clinical assays and for quality control in bioprocessing through examination of several analytical problems. The work also examined the development of automated methods of system preparation and sampling techniques to determine the partition coefficient in ATPS. The study demonstrated that the geometrical form of the phase diagram co-existence curve was of crucial importance since this directly affected the accuracy with which systems of defined Tie Line Length and Mass Ratio could be constructed. The TLL %Bias (accuracy) of a theoretical system range in the PEG1000-(NH4)2SO4 system at shorter TLL (12.2) was in the range +80.6% to -100% while at a longer TLL (53.1) the %Bias (accuracy) was reduced to +0.1% to -1.9%. At the same time the MR %Bias (accuracy) at shorter TLL (12.2) was in the range +59.5% to -21.3% while at the longer TLL (53.1) this was reduced to +2.7% to -2.6%. By contrast in the PEG8000-Dextran500 system the TLL %Bias (accuracy) at shorter TLL (13.1) was in the range +3.7% to -4.12%, while at a longer TLL (31.1) the range was +0.74% to -0.67%. The MR %Bias (accuracy) at the shorter TLL (13.1) was in the range +3.6% to -3% while at the longer TLL (31.1) the range was +1.1% to -1.4%. This illustrated that it is more difficult to work with a high degree of accuracy (e.g. %Bias <5%) close to the critical point in PEG-salt systems than in PEG-dextran systems. Two different approaches were taken to examine analytical phase partitioning. In the first approach the structure of the isoforms of a model protein (ovalbumin) were altered enzymatically. Analytical methods involving Strong Anion-Exchange chromatography were developed and applied to the separation of the ovalbumin isoforms. Removal of the phosphorylated groups (dephosphorylation of ovalbumin) was undertaken using alkaline phosphatase and de-glycosylation was attempted using neuraminidase and Endo-glycosidase F. However, both enzymatic approaches to deglycosylation were unsuccessful. Dephosphorylated isoforms were successfully produced and characterised. After partitioning in ATPS a clear difference was demonstrated between the behaviour of the native and dephosphorylated forms of ovalbumin. The mean % recovery in a PEG-salt ATPS was 99.8% (± 3.59) for the naive protein and 75.6% (± 4.03) for the dephosphorylated form. On the other hand, in a PEG3350-Dextran500 system, where solubility was maintained, a significant difference in the partition coefficient (K) of native and dephosphorylated ovalbumin was found. K for native ovalbumin was 0.85 while the partition coefficient of the dephosphorylated ovalbumin was 0.61. Analysis of covariance (ANCOVA) indicated that the regression coefficients of the respective partition isotherms were significantly different (p value < 0.05). In a second approach to examine analytical phase partitioning, chemical modification of a specific target surface amino acid of another model protein (serum albumin) was used to determine the degree of conjugation of the protein and also to determine its oxidative state. The method examined the reactivity of a free surface thiol to a wide range of labels ( (a) 2-methylsulfonyl-5-phenyl -1,3,4 oxidiazole reagent, (b) N-Ethylmaleimide (NEM) reagent, (c) 5, 5’-dithiobis (2-nitrobenzoate)(DTNB) (Ellman’s reagent), (d) N-pyrenylmaleimide (NPM) reagent, (e) Fluorescein-5-maleimide (F-5-M) Reagent). Only DTNB was found to modify the surface free thiol of serum albumin in a highly specific and quantitative manner. In the course of the development of a partitioning assay for surface free thiols of serum albumin significant oxidative properties were found to be associated with poly(ethylene glycol) PEG solutions and several attempts were made to find an oxidatively safe partitioning system by including antioxidants and by removal of contaminants by freeze drying. PEG3350-Dextran500 was found to provide an oxidatively safe environment for the development of a partitioning assay for the determination of albumin free thiols. A phase partitioning assay system capable of quantitatively resolving protein associated free thiols and low molecular weight thiols from a mixture of the two was developed. Correlation coefficients (R2) for the regression of experimentally determined protein free thiols in the presence of different levels of added LMW free thiol on the known addition of protein ranged from 0.77 to 0.83. The results demonstrated that the assay could quantify and distinguish both types of thiol in a simple two-step procedure.
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Buyel, Johannes Felix [Verfasser], and J. [Akademischer Betreuer] Hubbuch. "Overcoming Hurdles in Downstream Processing of Tobacco-derived Biopharmaceutical Proteins / Johannes Felix Buyel ; Betreuer: J. Hubbuch." Karlsruhe : KIT-Bibliothek, 2017. http://d-nb.info/1148551220/34.

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Dehling, Marco [Verfasser], Johannes [Akademischer Betreuer] Buchner, Matthias [Gutachter] Feige, and Johannes [Gutachter] Buchner. "Conformational analysis of proteins of biopharmaceutical interest / Marco Dehling ; Gutachter: Matthias Feige, Johannes Buchner ; Betreuer: Johannes Buchner." München : Universitätsbibliothek der TU München, 2018. http://d-nb.info/1153545853/34.

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Dehling, Marco Verfasser], Johannes [Akademischer Betreuer] [Buchner, Matthias [Gutachter] Feige, and Johannes [Gutachter] Buchner. "Conformational analysis of proteins of biopharmaceutical interest / Marco Dehling ; Gutachter: Matthias Feige, Johannes Buchner ; Betreuer: Johannes Buchner." München : Universitätsbibliothek der TU München, 2018. http://nbn-resolving.de/urn:nbn:de:bvb:91-diss-20180216-1404726-1-3.

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Arfi, Zulfaquar Ahmad Verfasser], Rainer [Akademischer Betreuer] [Fischer, and Stefan [Akademischer Betreuer] Schillberg. "Development of an immunoassay to detect tobacco host cell proteins during biopharmaceutical development / Zulfaquar Ahmad Arfi ; Rainer Fischer, Stefan Schillberg." Aachen : Universitätsbibliothek der RWTH Aachen, 2015. http://d-nb.info/1129176789/34.

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Arfi, Zulfaquar Ahmad [Verfasser], Rainer [Akademischer Betreuer] Fischer, and Stefan [Akademischer Betreuer] Schillberg. "Development of an immunoassay to detect tobacco host cell proteins during biopharmaceutical development / Zulfaquar Ahmad Arfi ; Rainer Fischer, Stefan Schillberg." Aachen : Universitätsbibliothek der RWTH Aachen, 2015. http://d-nb.info/1129176789/34.

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Books on the topic "Biopharmaceutical proteins"

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Spada, Stefania. Directory of approved biopharmaceutical products. Boca Raton: CRC Press, 2005.

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Approaches to the conformational analysis of biopharmaceuticals. Boca Raton: CRC Press/Taylor & Francis, 2010.

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Walsh, Gary. Post-translational modification of protein biopharmaceuticals. Weinheim: Wiley-VCH, 2009.

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Schmidt, Stefan R., ed. Fusion Protein Technologies for Biopharmaceuticals. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2013. http://dx.doi.org/10.1002/9781118354599.

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Jensen, Knud J., ed. Peptide and Protein Design for Biopharmaceutical Applications. Chichester, UK: John Wiley & Sons, Ltd, 2009. http://dx.doi.org/10.1002/9780470749708.

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Lene, Jorgensen, and Nielsen Hanne Mørck, eds. Delivery technologies for biopharmaceuticals: Peptides, proteins, nucleic acids, and vaccines. Chichester, West Sussex: John Wiley, 2009.

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N, Herron James, Jiskoot Wim, and Crommelin D. J. A, eds. Physical methods to characterize pharmaceutical proteins. New York: Plenum Press, 1995.

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GFP whole cell microbial biosensors: Scale-up and scale-down effects on biopharmaceutical processes. New York, N.Y: ASME Press, 2013.

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Thalmann, Beat. Identification of novel modulators towards high cell density and high-producing Chinese hamster ovary suspension cell cultures as well as their application in biopharmaceutical protein production. Berlin: Logos Verlag, 2015.

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NATO Advanced Research Workshop on Advanced Drug Delivery Systems for Peptides and Proteins (1986 Copenhagen, Denmark). Delivery systems for peptide drugs. New York: Plenum Press, 1986.

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Book chapters on the topic "Biopharmaceutical proteins"

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Fee, Conan J., and Vinod B. Damodaran. "Production of PEGylated Proteins." In Biopharmaceutical Production Technology, 199–222. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2012. http://dx.doi.org/10.1002/9783527653096.ch7.

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Bukowski, Ronald M. "Therapeutic Use of Recombinant Proteins." In Biopharmaceutical Drug Design and Development, 393–427. Totowa, NJ: Humana Press, 1999. http://dx.doi.org/10.1007/978-1-59259-705-5_15.

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Samuels, Michael. "Microarray Technology Using Proteins, Cells, and Tissues." In Biopharmaceutical Drug Design and Development, 67–97. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-532-9_5.

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Darling, Allan J. "Design and Interpretation of Viral Clearance Studies for Biopharmaceutical Products." In Downstream Processing of Proteins, 195–209. Totowa, NJ: Humana Press, 2000. http://dx.doi.org/10.1007/978-1-59259-027-8_15.

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Sejergaard, Lars, Haleh Ahmadian, Thomas B. Hansen, Arne Staby, and Ernst B. Hansen. "Model-Based Process Development in the Biopharmaceutical Industry." In Preparative Chromatography for Separation of Proteins, 429–55. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2017. http://dx.doi.org/10.1002/9781119031116.ch14.

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Corey, David R. "Design and Engineering of Proteins as Therapeutic Agents." In Biopharmaceutical Drug Design and Development, 187–203. Totowa, NJ: Humana Press, 1999. http://dx.doi.org/10.1007/978-1-59259-705-5_8.

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Jensen, Knud J. "De Novo Design of Proteins." In Peptide and Protein Design for Biopharmaceutical Applications, 207–48. Chichester, UK: John Wiley & Sons, Ltd, 2009. http://dx.doi.org/10.1002/9780470749708.ch6.

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Cheng, Kun, and Ram I. Mahato. "Biopharmaceutical Challenges: Pulmonary Delivery of Proteins and Peptides." In Pharmacokinetics and Pharmacodynamics of Biotech Drugs, 209–42. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2006. http://dx.doi.org/10.1002/9783527609628.ch9.

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Wei, Yangjie, Nicholas R. Larson, Gang Hu, Prashant Kumar, and C. Russell Middaugh. "Chapter 8: Biophysical Characterization and the Development of Therapeutic Proteins." In Development of Biopharmaceutical Drug-Device Products, 187–213. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-31415-6_8.

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Moussa, Ehab M., Tong Zhu, and Feroz Jameel. "Chapter 16: Development of Robust Lyophilization Process for Therapeutic Proteins: A Case Study." In Development of Biopharmaceutical Drug-Device Products, 391–403. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-31415-6_16.

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Conference papers on the topic "Biopharmaceutical proteins"

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Wang, You-Xin, Hong-Hong Fang, Zhong-Xin Xiao, Li-Juan Wu, Man-Shu Song, and Wei Wang. "Novel Method to Screen DNA Binding Proteins for a Given DNA Fragment." In 2015 International Conference on Medicine and Biopharmaceutical. WORLD SCIENTIFIC, 2016. http://dx.doi.org/10.1142/9789814719810_0093.

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Ao, Pei. "ATP Binding Residues of Proteins Ensemble Prediction Based on Imbalanced Data Sets." In 2015 International Conference on Medicine and Biopharmaceutical. WORLD SCIENTIFIC, 2016. http://dx.doi.org/10.1142/9789814719810_0107.

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Khan, Mohammed, Xiaolin Chen, and Jie Xu. "Separation of Non-Viable Chinese Hamster Ovary (CHO) Cells Using Dielectrophoresis in a Deterministic Lateral Displacement Ratchet." In ASME 2020 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2020. http://dx.doi.org/10.1115/imece2020-23520.

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Abstract Chinese hamster ovary (CHO) cell is the most widely used mammalian cell line for commercial production of therapeutic protein. Any presence of non-viable cells in culture medium may adversely affect subsequent functionality of these proteins. Therefore, separation of non-viable cells from suspending medium is critical in biopharmaceutical and biomedical sectors. One such method termed Deterministic Lateral Displacement has already shown promising capabilities in separating cells based on the cell size difference by taking advantage of the predictable flow laminae. However, in cases where size overlaps between viable and non-viable cells are present, separation based solely on size suffers and high-resolution separation techniques are required. Dielectrophoresis, one of the most widely used nonlinear electro-kinetic mechanism, has the potential to manipulate the same size cells depending on the dielectric properties of individual cells. In this work, we demonstrated that a DLD device can be combined with a frequency-based AC electric field to perform high resolution continuous separation of non-viable CHO cells from the viable or productive cells. The behavior of the coupled DLD-DEP device is further investigated by employing numerical simulation to check the effect of geometrical parameters of the DLD arrays, velocities of the flow field and required applied voltages. A moderate row shift fraction with velocity 700μm/s provided a good separation behavior without any trapping. The cell viability was also ensured by maintaining proper electric field which otherwise may cause cell loss due to ion leakage. Our developed numerical model and presented results lay the groundwork for design and fabrication of high resolution DLD-DEP microchips for enhanced separation of viable and nonviable cells.
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Song, Xiao-Lei, Yan Liu, Li Wei, Jian Yu, and Chun-Xia Wang. "Immobilization of Trypsin on Filter Paper for Protein Digestion." In 2015 International Conference on Medicine and Biopharmaceutical. WORLD SCIENTIFIC, 2016. http://dx.doi.org/10.1142/9789814719810_0112.

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Hou, Li-Xia, Ying-Ying Wang, Yu-Lan Liu, and Xiao-Kun Wang. "Effect of Sonication on Proteolysis of Peanut Protein Isolate." In 2015 International Conference on Medicine and Biopharmaceutical. WORLD SCIENTIFIC, 2016. http://dx.doi.org/10.1142/9789814719810_0147.

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Liu, Chang, Fang-Jie Li, Han-Bo Xiao, Ling Hai, and Song-Yi Lin. "Optimization on Production Process of Soybean Protein Hydrolysates Chelating Calcium." In 2015 International Conference on Medicine and Biopharmaceutical. WORLD SCIENTIFIC, 2016. http://dx.doi.org/10.1142/9789814719810_0157.

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Yang, Fan, Hong-Liang Liu, Xiao-Wan Liu, Bo Guo, Song Li, Ping Li, and Ling Zhug. "Development of a TTSuV2-ORF1 Protein-based Indirect Blocking ELISA for Serological Testing." In 2015 International Conference on Medicine and Biopharmaceutical. WORLD SCIENTIFIC, 2016. http://dx.doi.org/10.1142/9789814719810_0023.

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Guo, Chun-Rong, Fu-Feng Li, Zhu-Mei Sun, Peng Qian, Wei-Fei Zhang, Dan Chen, Yuan Zhao, Hai-Yang Jiang, and Xi-Chen Cai. "Effect of Ping-Chuan-Fang on TGF-β1, Smad and ADAM33 Protein Expression in Chronically Asthmatic Rats." In 2015 International Conference on Medicine and Biopharmaceutical. WORLD SCIENTIFIC, 2016. http://dx.doi.org/10.1142/9789814719810_0017.

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Liu, Chun-Lei, Bai-Ying Cao, Wei-Hong Min, Jing-Sheng Liu, Li Fang, Hong-Mei Li, and Jing-Jing Li. "Proteomic Analysis of Pine Nut (Pinus Koraiensis Sieb. et Zucc) Protein in Changbai Mountain by Shotgun Approach." In 2015 International Conference on Medicine and Biopharmaceutical. WORLD SCIENTIFIC, 2016. http://dx.doi.org/10.1142/9789814719810_0183.

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Liu, Tao, Qiu-Ling Xu, Zhao-Xin Yang, and Yan Zhao. "Emodin Protects NAFLD Rats via Regulating the Genes Expression of Hepatic TLR4 Genes." In 2015 International Conference on Medicine and Biopharmaceutical. WORLD SCIENTIFIC, 2016. http://dx.doi.org/10.1142/9789814719810_0069.

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