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Dive into the research topics where Jennifer M. Pollard is active.

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Featured researches published by Jennifer M. Pollard.


Biotechnology Progress | 2014

A practical strategy for using miniature chromatography columns in a standardized high-throughput workflow for purification development of monoclonal antibodies

John P. Welsh; Matthew Petroff; Patricia Rowicki; Haiying Bao; Thomas O. Linden; David J. Roush; Jennifer M. Pollard

The emergence of monoclonal antibody (mAb) therapies has created a need for faster and more efficient bioprocess development strategies in order to meet timeline and material demands. In this work, a high‐throughput process development (HTPD) strategy implementing several high‐throughput chromatography purification techniques is described. Namely, batch incubations are used to scout feasible operating conditions, miniature columns are then used to determine separation of impurities, and, finally, a limited number of lab scale columns are tested to confirm the conditions identified using high‐throughput techniques and to provide a path toward large scale processing. This multistep approach builds upon previous HTPD work by combining, in a unique sequential fashion, the flexibility and throughput of batch incubations with the increased separation characteristics for the packed bed format of miniature columns. Additionally, in order to assess the applicability of using miniature columns in this workflow, transport considerations were compared with traditional lab scale columns, and performances were mapped for the two techniques. The high‐throughput strategy was utilized to determine optimal operating conditions with two different types of resins for a difficult separation of a mAb monomer from aggregates. Other more detailed prediction models are cited, but the intent of this work was to use high‐throughput strategies as a general guide for scaling and assessing operating space rather than as a precise model to exactly predict performance.


Engineering in Life Sciences | 2016

High-throughput techniques to evaluate the effect of ligand density for impurity separations with multimodal cation exchange resins

John P. Welsh; Haiying Bao; Kenneth Barlow; Jennifer M. Pollard; Eggert Brekkan; Karol Lacki; Thomas O. Linden; David J. Roush

Scale‐down, high‐throughput screening techniques are well on their way to becoming a commodity in downstream bioprocess development, especially for the rapid development of chromatography process steps. This work used both resin slurry plate and miniature column high‐throughput screening methodologies to identify the best resin properties for mAb separations utilizing a multimodal chromatography ligand interaction. A ligand with both cation exchange and hydrophobic interaction properties was studied at several ligand densities and compared to a commercially available multimodal resin with a larger particle size at high ligand density. The resins were screened with mAbs containing distinct process impurities (aggregates and a hydrophobic variant), and optimized conditions provided more than a log of clearance of both types of impurities for the different resins screened. These studies reveal that while a smaller particle size is generally preferable, optimal ligand densities can be different depending on the properties of both the mAb and impurity studied.


Engineering in Life Sciences | 2016

Lessons learned in building high-throughput process development capabilities

Jennifer M. Pollard; Paul J. Mcdonald; Ashley Hesslein

Companies have adapted high‐throughput techniques for process development to different levels. Some companies are beginning to incorporate high‐throughput process development (HTPD) techniques at a level which is approachable for the beginner user (example: plate‐based resin screening for purification) and others have sophisticated robotic platforms which are in routine use for new pipeline products for upstream, downstream, analytics, and just now starting in the protein formulation area. This mini review serves to summarize how companies have set up and are using HTPD capabilities, including the need for user‐groups to improve the likelihood of success. The focus will be a practical summary of the utility and limitations of these approaches.


Engineering in Life Sciences | 2016

Domain antibody downstream process optimization: High-throughput strategy and analytical methods

John P. Welsh; Michael A. Rauscher; Haiying Bao; Sandra Meissner; InKwan Han; Thomas O. Linden; Jennifer M. Pollard

Application of scale‐down high‐throughput screening has become integral for process development of antibody therapeutic products. In this work, methods are described for using high‐throughput techniques to develop a multicolumn chromatography purification protocol for a small domain antibody with very limited material (<200 mg). Screenings utilized resin slurry plates to explore and narrow potential operating space, and miniature columns were used to either confirm operating spaces or further explore impurity separations. Lab scale column confirmations were performed when appropriate. Affinity capture chromatography as well as ion exchange and multimodal polishing chromatography steps were explored. Feedstreams were pooled and recycled to preserve material for the different chromatography steps. Precise high‐throughput analytical assays were developed to fully characterize the domain antibody to a similar extent as a typical commercial therapeutic protein program. Optimized two‐column and three‐column processes provided overall chromatography yields of 66 and 58%, respectively, and were able to meet typical early phase requirements for removal of impurities such as aggregates, host cell protein, endotoxin, and other product‐related impurities. This study provides a comprehensive example of how a thorough biologics downstream process can be developed with a minimum of material.


Journal of bioprocessing & biotechniques | 2014

Demonstrating β-glucan Clearance in CHO- and Yeast-Produced Monoclonal Antibodies during Downstream Purification Processes

Fengqiang Wang; Hong Li; Zhi Chen; John P. Welsh; Douglas Richardson; Jennifer M. Pollard; Daisy Richardson; Mohammed Shameem

Biologics production using yeast or CHO with Yeastolate as cell culture additives often introduces β-glucan, which could potentially pose immunogenicity risk, if not adequately removed. Although a previous study has shown the effective clearance of Yeastolate-derived β-glucan by Protein A chromatography, the clearance pattern of yeast cell derived β-glucan remains unknown. In this study, we characterized the β-glucan clearance patterns during downstream processing of three monoclonal antibody (mAb) products, one mAb fragment from Pichia pastoris (mAb A) and two full mAbs from CHO expression system (mAb B and mAb C), by Glucatell assay. We demonstrated effective β-glucan clearance in both small (100 L) and large scale (5000 L) batches of mAb A as well as in one batch of mAb B. Protein A purification step removed an average of 97.74% (1.7 log10 reduction) of β-glucan detected in the two batches of mAb A microfiltration permeates (MFP) and 99.99% (3.9 log10 reduction) of β-glucan detected in mAb B clarified culture fluid harvest (HCCF). Residual β-glucans post Protein A purification in the two batches of mAb A were further removed by the two polishing chromatography steps (94.76% reduction on average). Residual β-glucan measured in the mAb A and mAb B drug substance ranges from 7.8 to 19 pg/mg, which is unlikely to alter physiological concentrations significantly in healthy adults when administered with typical intravenous doses. However, in mAb C, after almost complete removal (99.99%) by Protein A purification step, β-glucan level increased more than 20 fold in Viral Filtration (VF) product sample, indicating that it can be introduced from materials used in downstream process, such as cellulose-based filters and membranes. Our study results suggest that although β-glucan can be cleared by Protein A and other chromatographic steps such as AEX, monitoring β-glucan clearance during downstream process development remains very important to identify and avoid potential contaminations to the drug substance.


Biotechnology and Bioengineering | 2016

High throughput chromatography strategies for potential use in the formal process characterization of a monoclonal antibody

Matthew Petroff; Haiying Bao; John P. Welsh; Miranda van Beuningen – de Vaan; Jennifer M. Pollard; David J. Roush; Sunitha Kandula; Peter Machielsen; Nihal Tugcu; Thomas O. Linden

High throughput experimental strategies are central to the rapid optimization of biologics purification processes. In this work, we extend common high throughput technologies towards the characterization of a multi‐column chromatography process for a monoclonal antibody (mAb). Scale‐down strategies were first evaluated by comparing breakthrough, retention, and performance (yields and clearance of aggregates and host cell protein) across miniature and lab scale columns. The process operating space was then evaluated using several integrated formats, with batch experimentation to define process testing ranges, miniature columns to evaluate the operating space, and comparison to traditional scale columns to establish scale‐up correlations and verify the determined operating space. When compared to an independent characterization study at traditional lab column scale, the high throughput approach identified the same control parameters and similar process sensitivity. Importantly, the high throughput approach significantly decreased time and material needs while improving prediction robustness. Miniature columns and manufacturing scale centerpoint data comparisons support the validity of this approach, making the high throughput strategy an attractive and appropriate scale‐down tool for the formal characterization of biotherapeutic processes in the future if regulatory acceptance of the miniature column data can be achieved. Biotechnol. Bioeng. 2016;113: 1273–1283.


Engineering in Life Sciences | 2016

High‐throughput purification tools for rapid upstream process development are interchangeable for biologics

Matthew Petroff; Jessika Feliciano; David Pollard; Hong Li; Thomas O. Linden; Jennifer M. Pollard

Upstream process development of biologics is not only productivity‐driven but also quality‐driven. Typically, most quality attributes are not directly measurable in cell culture samples due to low product concentration and purity, thus requiring some level of sample purification. As higher throughput upstream technologies become available, sample purification is becoming a bottleneck in limiting the number and types of cell culture samples that can be analyzed. The application of high‐throughput, microscale protein purification techniques has the potential to address and expand this capability. In this work, the affinity capture step of an IgG1 mAb was adapted to fit resin‐plate, resin‐tip, and mini‐column formats in an attempt to approximate the packed‐column performance by optimizing parameters such as contact time, liquid/resin ratio, and loading to produce a yield of ≥70% yield. A representative cell culture supernatant was purified using both the optimized microscale and conventional techniques, and analyzed using a comprehensive panel of product quality assays. This direct comparison demonstrated that each technique generates product of equivalent purity across a wide range of feed conditions. The analytical comparability suggests that any of the conventional and high‐throughput methods are interchangeable for biologics, allowing flexible development of an end‐to‐end integrated high‐throughput strategy.


Tetrahedron-asymmetry | 2006

Effective synthesis of (S)-3,5-bistrifluoromethylphenyl ethanol by asymmetric enzymatic reduction

David Pollard; Matthew D. Truppo; Jennifer M. Pollard; Cheng-yi Chen; Jeffrey C. Moore


Journal of Chemical & Engineering Data | 2006

Solubility and partitioning behavior of surfactants and additives used in bioprocesses

Jennifer M. Pollard; and Jie Shi; Kent E. Göklen


Archive | 2017

Lab-Scale Development of Chromatography Processes

Hong Li; Jennifer M. Pollard; Nihal Tugcu

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