Biophysical and Structural Analysis

 

Biophysical and structural analysis are now playing increasingly important roles in the discovery and development of next generation biotherapeutics. Developability assessment is now standard practice across the industry, and understandings gained at this step are now being applied in the optimization of candidates at early stages of the pipeline. Higher resolution tools are enabling better understandings of how to characterize and control aggregation and particulates and are increasingly allowing these methods to be used in a quantitative, rather than qualitative way. The PEGS “Biophysical and Structural Analysis” conference brings together an international audience of protein scientists and analytical specialists to explore the latest technologies and methods for problem solving in this dynamic field and identify ways of optimizing the studies performed in support of regulatory filings and manufacturing.

Final Agenda

WEDNESDAY, APRIL 10

7:15 am Registration (Commonwealth Hall) and Morning Coffee (Harbor Level)

7:25 - 8:25 PANEL DISCUSSION: Women in Science – Inspired Professional and Personal Stories (Continental breakfast provided) (Waterfront 1&2)

Moderator:

Jennifer-ChadwickJennifer S. Chadwick, PhD, Director of Biologic Development, BioAnalytix, Inc.; Co-Chair, Mentors Advisors and Peers Program, Women In Bio, Boston Chapter


Panelists:

Joanna BrewerJoanna Brewer, PhD, Vice President, Platform Technologies, AdaptImmune


Charlotte A. RussellCharlotte A. Russell, MD, DMSc, CMO, Alligator Bioscience


Susan RichardsSusan Richards, PhD, Presidential Scientific Fellow, Translational Medicine Early Development, Sanofi R&D


Kristi SarnoKristi Sarno, Senior Director, Business Development, Pfenex


CHARACTERIZING HIGHER ORDER STRUCTURE

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8:30 Chairperson’s Opening Remarks

Jessy Fan, PhD, Scientist, Amgen

8:40 Characterization of Therapeutic Proteins by Circular Dichroism Spectroscopy: Application to Process Comparability and Establishment of Critical Quality Attributes

Balakrishnan_GarusamyGurusamy Balakrishnan, PhD, Scientist, Bristol-Myers Squibb

Circular dichroism (CD) spectroscopy is a widely used technique for assessing protein higher order structure (HOS) but remains difficult to assess HOS with high fidelity due to lack of sensitivity towards subtle structural perturbations. This presentation will discuss these challenges and an effective experimental method for CD measurements with the relevant examples from analytical comparability for process change and forced degradation studies for establishing critical quality attributes.

9:10 Ion Mobility Spectrometry Mass Spectrometry (IMS-MS) for HOS Characterization

Ruotolo_BrandonBrandon Ruotolo, PhD, Professor, Chemistry, University of Michigan

The next generation of medicines will rely heavily upon our ability to quickly assess the structures and stabilities of large, complex macromolecular machines, as well as the influence of large libraries of conformationally-selective small molecule binders and protein-based biotherapeutics. Such endeavors are nearly insurmountable with current tools. In this presentation, I will discuss recent developments in ion mobility-mass spectrometry (IM-MS) technology that seek to bridge this gap.

9:40 Keynote Presentation: The Underestimated Power of Well-Established Methods to Assess Protein Higher Order Structure

Carpy_AlejandroAlejandro Carpy, PhD, Head, Senior Scientist, Large Molecule Research, Roche Innovation Center Munich, Germany

Proper higher order structure (HOS) is essential for the function and stability of biologics. A large number of biochemical or biophysical methods are available to assess HOS, which differ in sensitivity and specificity. We will show that approaches based on combination of conventional methods such as bioassays or liquid chromatography, which are used for batch release, are well-suited and sufficient to assess HOS, especially during early clinical development.

10:10 Coffee Break in the Exhibit Hall with Poster Viewing (Commonwealth Hall)

10:15 Women in Science Speed Networking in the Exhibit Hall (Commonwealth Hall)

IMPLEMENTING THE MULTI-ATTRIBUTE METHOD (MAM)

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10:55 MAM Method Development and Qualification

Wang_JihongJihong Wang, PhD, Principal Scientist, AstraZeneca

Several multi-attribute monitoring methods (MAM) have been developed in the biopharmaceutical industry in recent years. We reported MAM method based on Quadrupole Dalton (QDa) mass detector to selectively monitor and quantitate PTMs in a therapeutic monoclonal antibody. In this talk, case studies will be presented on applications and implementation of QDa-based QC friendly MAM methods from supporting process characterization to product release.

11:25 Implementing the Multi-Attribute Method in a Multi-Site Analytical Development Organization: Successes and Challenges

Boggio_KristinKristin Boggio, PhD., Senior Scientist, Protein Mass Spectrometry, Pfizer

Biotherapeutics development requires thorough understanding of product quality attributes (PQAs) to ensure that clinical materials meet the desired safety/efficacy profile. Numerous routine assays are used to characterize and monitor PQAs; however, execution of multiple methods becomes time and resource intensive, often providing indirect measurements of biologically-relevant PQAs. We have incorporated the mass spectrometry-based multi-attribute method at various stages in non-GMP product development to monitor multiple PQAs within a single experiment.

11:55 Development of MS-Based Multi-Attribute Methods for ADC Process Support

Wang_LintaoLintao Wang, Ph.D., Associate Director, Analytical and Pharmaceutical Development, ImmunoGen, Inc.

Antibody-drug conjugates (ADCs) are complex anti-cancer biomolecules that have multiple quality attributes. A mass spectrometry based multi-attribute method (MAM) was developed for monitoring quality attributes (such as deamidation, oxidation, glycosylation, disulfide mispairing, etc.) to support process development of an ADC with engineered cysteine linkage.

12:25 pm A Three-Pronged Characterization Tool That Makes Unstable Proteins Cry “Uncle”

Kevin Lance, PhD, Product Manager, Marketing, Unchained Labs

Optimizing protein stability and developing the best formulations for avoiding aggregation is important throughout the biologics development pathway.  Uncle’s unique combination of static light scattering, dynamic light scattering, and fluorescence gives you the flexibility needed to tease out the right answers and understand the whole story.

12:55 Luncheon Presentation I: The Perfect Recipe for Protein Characterization Starts with Tycho and Knowing Protein Quality

Peter A. Fung, Senior Manager Product Marketing, NanoTemper Technologies

Starting with material of questionable quality for protein purification and characterization leads to irreproducible or ambiguous results. Tycho tells you so much about the quality of your protein—its presence, purity, concentration, functionality and similarity — in a single experiment. These can all be measured simply by determining whether your protein is structurally intact or properly folded. Tycho fits into any step of a purification or characterization workflow to easily monitor protein quality and help researchers to get more consistent results.

Halo-Labs
1:25 
Luncheon Presentation II: High Throughput Low Volume Subvisible Particle Analysis

John Proctor, PhD, Vice President, Marketing, Halo Labs

Subvisible particle analysis is a key predictor of protein drug stability and an essential drug product quality metric. Currently it is almost impossible to obtain this vital info during early stage formulation development.  Come see how the new HORIZON system from Halo Labs uses Backgrounded Membrane Imaging (BMI) to measure subvisible particles, including translucent protein aggregates. The measurement is fully automated for up to 96 samples and uses 1/10th the volume of other techniques.

1:55 Session Break

METHODS AND INSTRUMENTS

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2:10 Chairperson’s Remarks

Brandon Ruotolo, PhD, Professor, Chemistry, University of Michigan

2:15 Leveraging Force Degraded Material to Increase the Throughput of Peptide Map Characterization

Rao_RomeshRomesh Rao, Research Associate, Analytical Sciences, Seattle Genetics

Appropriately degraded samples can increase the throughput of peptide map characterization by facilitating data analysis. Post-translational modifications (PTMs) in a highly degraded sample were identified and site localized, enabling rapid, site-specific assignments of PTMs during subsequent analysis of nominal samples by comparison. This approach can also support lower resolution, higher throughput workflows.

2:45 PULSE-SPR and its Applications in Developability Assessment

Zhou_LiLi Zhou, PhD, Senior Scientist, Global Biologics, AbbVie

Downstream purification of therapeutic antibodies requires candidates to be stable under various stress conditions such as low pH. Here we report a high throughput method that measures protonation induced unfolding of ligand binding sites for stability evaluation by surface plasmon resonance, or PULSE SPR.

3:15 Advances in High-Throughput Screening for Development and Formulation of Biologics

Champagne_JohnJohn Champagne, PhD, Senior Applications Scientist, Northeast Regional Manager, Sales, Wyatt Technology

Light scattering addresses many key analytical challenges in drug nanoparticle R&D, including accurate size distributions, conformation, payload, and formulation. We review light scattering fundamentals and then present examples illustrating how. Wyatt’s unique light scattering instrumentation facilitates rapid and effective development of controlled release vehicles including liposomes, VLPs, polymer-encapsulated nanoparticles, and nanogels.

3:45 Refreshment Break in the Exhibit Hall with Poster Viewing (Commonwealth Hall)

4:45 Problem-Solving Breakout Discussions - Click here for details(Commonwealth Hall)

5:45 Networking Reception in the Exhibit Hall with Poster Viewing (Commonwealth Hall)

7:00 End of Day

THURSDAY, APRIL 11

8:00 am Registration (Commonwealth Hall) and Morning Coffee (Harbor Level)

SPECTROMETRY METHODS

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8:30 Chairperson’s Remarks

Iain D. G. Campuzano, Principal Scientist, Discovery Attribute Sciences, Amgen

8:35 Cutting-Edge Chromatographic, Electrophoretic and Mass Spectrometry of mAbs, Fc-Fusion Proteins and ADCs

Beck_AlainAlain Beck, PhD, Senior Director, Biologics CMC and Developability, Pierre Fabre Laboratories, France

Developability and comparability assessment of current and next generation of biologics such as engineered mAbs, Fc-fusion proteins, BsAbs and 2 or 3G-ADCs requires state-of-the-art analytical and structural methods. Case studies will be presented based on native and ion mobility MS, multi-level 2- to 4 LC-MS, multiplexed Top and Middle-Down MS, multiple fragmentation techniques, comprising high energy collisional-, electron-transfer and ultraviolet photo-dissociation (HCD, ETD and UVPD) and CE-MS.

9:05 The Application of Fourier Transform Ion Cyclotron Resonance MS and Spectral Deconvolution Algorithms within Biopharma Research

Campuzano_IainIain D. G. Campuzano, Principal Scientist, Discovery Attribute Sciences, Amgen

Native-MS analyses for accurate antibody, protein and nanodisc MW and DAR confirmation have traditionally been performed using oa-ToF instrumentation and more recently the extended mass range Orbitrap analyzer with incremental improvements in data quality. Analysis of mAbs, ADCs, nanodiscs and a PEGylated biotherapeutics used FT-ICR MS under both native and denaturing LC-MS conditions. Also demonstrated is the use of a new parsimonious deconvolution algorithm that can efficiently deconvolve highly polydisperse MS spectra.

9:35 Considerations of the Use of Analytical Ultracentrifugation for Characterization of AAV Gene Delivery Vectors

Sucato_ChristopherChristopher Sucato, PhD, Senior Scientist, Biophysical Characterization, Charles River

Analytical Ultracentrifugation (AUC) in the biopharmaceutical industry has traditionally been employed in the analysis of aggregation and higher order structure in protein drug products, where monomeric or dimeric protein is commonly the analyte. More recently, the rise of gene delivery vectors as a means to treat a number of conditions has opened new avenues for AUC-based characterization and QC lot release methodologies.

10:05 Coffee Break in the Exhibit Hall with Poster Viewing (Commonwealth Hall)

AGGREGATION AND STABILITY

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11:05 Ultrafast High-Resolution Protein Analysis Unconventional Devices

Ghosh_RajaRaja Ghosh, PhD, Professor, Chemical Engineering, McMaster University, Canada

High-speed, high-resolution analytical separation is one of the current needs with biopharmaceuticals. Separations using ultrafine particulate chromatographic media require ultra-high pressures which could have detrimental effects on the molecules being analyzed. In this presentation, membrane-based devices suitable for rapid, high-resolution analytical protein separation are discussed. Using these devices, high-resolution separation of proteins could be carried out in minutes at less than 1 MPa backpressure.

11:35 Effect of L-proline, L-arginine.HCl and NaCl on the Aggregation and Viscosity Behavior of High-Concentration Antibody Formulations

Sudrik_ChaitanyaChaitanya Sudrik, PhD, Postdoctoral Associate, Molecular Engineering, Massachusetts Institute of Technology

Development of subcutaneous formulations for monoclonal antibodies is hindered by several physical instabilities. In this study, we compare preferential interactions of L-proline, L-arginine.HCl and NaCl with the native state of three IgG1 mAbs that differ in their physical stability attributes. We also highlight differences amongst the excipients in terms of their effect on the aggregation and viscosity of these antibodies at high protein concentration.

12:05 pm Impact of Non-Ideal Analyte Behavior on the Separation of Protein Aggregates by Asymmetric Flow Field-Flow Fractionation

Boll_BjörnBjörn Boll, Ph.D., Head, Particle Lab and Higher Order Structure Protein Analytics, Novartis Pharma AG, Switzerland

Asymmetric flow field-flow fractionation (AF4) is a valuable tool for the characterization of protein aggregates owing to its broad size range and unique separation principle. In practice, AF4 is non-trivial to use due to deviations from theory. This presentation gives an overview about non-ideal effects that influence AF4 separation including new approaches to minimize non-ideal behavior and drastically improving AF4 resolution by adjusting the mobile phase.

12:35 End of Biophysical and Structural Analysis


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