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Monday October 19 Breakfast Seminars
Mild Protein A Purification with Digital Membrane Chromatography (DMC): From Rapid Sample Preparation for Analytical Characterization to Reduced Aggregation Risk for Complex Antibodies
Presented By: Jane Jones
Protein A affinity purification is frequently used to prepare antibody samples for analytical characterization, but conventional workflows can require low-pH elution, immediate neutralization, buffer exchange, and concentration before analysis. These additional steps increase processing time, create opportunities for sample loss, and may alter pH-sensitive molecules before their biophysical properties are measured.
Digital Membrane Chromatography (DMC) combines a Protein A membrane adsorber with electrically controlled elution, enabling captured antibodies to be recovered rapidly into a selected buffer without conventional acidic elution.
This presentation examines DMC Protein A as a rapid sample-preparation tool for biophysical and analytical methods. Early data indicate that DMC-purified samples can be compatible with direct injection into mass spectrometry workflows, reducing the number of steps between sample preparation and analysis. By eliminating neutralization and reducing or avoiding desalting and buffer-exchange requirements, DMC can shorten turnaround time, reduce sample handling, and improve workflow efficiency.
Beyond rapid sample preparation, the alternative elution principle of DMC offers particular advantages for the purification of antibody–drug conjugates, bispecific and multispecific antibodies, and other complex antibody formats. For molecules sensitive to the acidic conditions typically used for Protein A elution, DMC eliminates low-pH exposure during elution, thereby reducing purification-induced aggregation and increasing monomeric yield compared with conventional Protein A purification. This mild elution approach helps preserve valuable antibody material for subsequent binding, potency, and developability studies.
Together, these findings support Protein A DMC as a complementary platform for rapidly preparing assay-ready antibody samples while also enabling mild capture of complex therapeutic candidates during early discovery and developability studies.
Mastering the art of oligonucleotide analysis via LCMS using the HALO 1000Å OLIGO C18 HPLC column
Presented By: Josh McBee Ph.D.
Oligonucleotide-based therapeutics are a rapidly growing area that present unique challenges for analytical analysis. LC/MS has excellent utility for performing critical quality attribute (CQA) testing but can present several novel hurdles for MS users accustomed to performing routine small molecule, protein, or peptide analysis. Their large size, hydrophilic nature and separation challenges require unique approaches.
This seminar will demonstrate how to build an ion pair/reversed phase (IP/RP) LC/MS workflow using our novel HALO 1000Å OLIGO C18 HPLC columns. We will discuss proper sample prep and handling, ion pairing reagent selection and procedures for making IP buffers, and how to minimize adduction risk when performing MS analysis.
We will show several applications including siRNA impurity analysis and sgRNA’s for CRISPR applications.
We hope this seminar will provide MS users with confidence in approaching oligonucleotide analysis and a framework for proper method development.
Monday October 19 Lunch Seminars
Vaast: Expanding the Chiral Separation Toolbox: Technologies and
Applications for Challenging Separations
Presented By: Dr. Weston J. Umstead
Chiral separations encompass a broad range of compounds and applications, and differences in molecular structure can lead to substantially different requirements for stereochemical recognition. Consequently, a diverse range of chiral stationary phase technologies have been developed to provide complementary selectivity across different separation challenges. This seminar will provide an overview of the chiral separation technologies available from Daicel, beginning with a brief introduction to the mechanisms responsible for chiral recognition and the role of complementary stationary phase selectivity. The discussion will then survey Daicel’s portfolio of polysaccharide-based and specialty chiral stationary phases, highlighting their distinguishing characteristics, chromatographic capabilities, and representative areas of application. Examples spanning small molecules, amino acids, peptides, pharmaceutical compounds, and other stereochemically complex analytes will illustrate the breadth of applications these technologies enable. Practical considerations including available separation modes, column formats, method development resources, and technical support will also be discussed. The seminar is intended to provide attendees with a broad understanding of the chiral separation tools currently available, the types of challenges each technology can address, and resources available to support the development of new chiral separations.
From Injection to Detection: Leveraging Advanced LC and MS Technologies for Therapeutic Peptide Characterization
Presented By: William Levandowski
As interest in therapeutic peptides continues to grow, there is an increasing need for analytical workflows that provide flexible, robust, and comprehensive methods for their characterization. This presentation highlights an integrated approach covering multiple chromatographic
techniques using the Agilent 1290 Infinity III LC series and Pro iQ MS Platform to provide comprehensive characterization of GLP-1 peptides. Through the use of advanced sample introduction capabilities and complementary detection methods, the workflows presented support routine analysis while accommodating diverse sample conditions and analytical challenges. The results demonstrate a practical strategy for obtaining reliable, high-quality data, enabling confident decision-making throughout peptide analysis and development workflows.
Tuesday October 20 Breakfast Seminars
Integrated and intensified downstream processing within a continuous multi-column chromatography platform
Presented By: Abbie Breton
Achieving true continuity in downstream processing remains a key challenge for monoclonal antibody (mAb) production. Here, multi-column chromatography (MCC) is advanced beyond continuous capture to enable direct integration of a subsequent chromatographic purification step on a single system.
Previous integration of downstream steps has been constrained by equipment and process limitations. The adapted multi-column system used in this work integrates two chromatographic steps in a single 8-column setup, supporting uninterrupted operation and efficient resin use.
Using a high alkaline stable, fast kinetic ligand, and high dynamic binding capacity (DBC) Protein A affinity resin, we demonstrate robust mAb capture and subsequent polishing with a highly salt-tolerant cation exchange resin, advancing practical implementation of end-to-end continuous purification. In addition, a low-threshold pH step was applied into this process integration to achieve inline virus inactivation. A high degree of automation has been achieved with this setup, while the footprint has been reduced both by reducing the size of the systems and by saving on cost of buffers, thereby making downstream processing more sustainable.
Tuesday October 20 Lunch Seminars
