CONFERENCE SERIES: Biological Therapeutic Products
Recorded at: PepTalk: The Protein Science Week
Digital Course: Characterization and Analysis of Particulates
About this Product:
Sub-visible particles present in these products are a product quality attribute and a potential patient safety concern yet to be fully explored. Early and consistent particle detection, quantitation and control throughout the product life cycle of these drugs from development to commercial lot release is critical in mitigating any concerns. This requires appropriate analytical methods which can be applied to biopharmaceuticals across a large variety of protein concentrations and modes of administration. This digital course and interactive discussion will cover strategies to utilize complementary methods and techniques at different phases of product development.
Rational Design of Protein Solutions
Thomas M. Laue, Ph.D.
Nick Pace, Ph.D.
About this Product:
Over 113 Slides
Individual Copy: $345
Site License: $1380
Agenda At A Glance:
Sub-visible particles present in these products are a product quality attribute and a potential patient safety concern yet to be fully explored. Early and consistent particle detection, quantitation and control throughout the product life cycle of these drugs from development to commercial lot release is critical in mitigating any concerns. This requires appropriate analytical methods which can be applied to biopharmaceuticals across a large variety of protein concentrations and modes of administration. This workshop and interactive discussion will cover strategies to utilize complimentary methods and techniques at different phases of product development.
Chair: Danny Chou, Ph.D., Bioprocess Analytical Scientist, Genzyme
Instructors: Kevin Mattison, Ph.D., Principal Scientist Bioanalytics, Malvern Instruments
Danny Chou, Ph.D., Bioprocess Analytical Scientist, Genzyme
Dr. Chou is a Bioprocess Analytical Scientist at Genzyme Corportion. He has technical experience in therapeutic protein formulation development as well as strategies for increasing protein solubility, stability and elucidation of protein aggregation/self-association and degradation mechanisms. His expertise is in the study of protein-protein and ligand-protein interactions using laser light scattering, isothermal titration calorimetry (ITC) as well as fluorescene spectroscopy. Protein formulation, fill & finish process development, bioprocess development, analytical method development, technology transfer, and manufacturing support are a few of his specialties. Dr. Chou received his PhD in Pharmaceutical Biotechnology at the University of Colorado at Denver.
Kevin Mattison, Ph.D., Principal Scientist Bioanalytics, Malvern Instruments
Dr. Mattison completed his doctorate in biological chemistry at Purdue University, where he studied the effects of polyelectrolyte additives on the stability and activity of transport proteins and enzymes. From there he joined Protein Solutions as the Applications Development and Technical Support Manager, and was instrumental in helping to drive the adoption of sub-micron light scattering techniques from esoteric technologies into main stream laboratory tools. In 2002 Dr. Mattison joined Malvern Instruments, where he served as Applications Manager, Product Manager, and Director of Customer Support, prior to assuming his current position as Principal Scientist – Bioanalytics in the Strategic Technology Development Group.
This digital course includes two bonus presentations including: "Overview on Colloidal Versus Molecular Solution Stability" delivered by Thomas M. Laue, Ph.D., Professor, Biochemistry and Molecular Biology; Director, Biomolecular Interaction Technologies Center (BITC), University of New Hampshire and “Increasing Protein Stability and Solubility” delivered by C. Nick Pace, Ph.D., Professor, Medical Biochemistry and Genetics and of Biochemistry and Biophysics, Texas A&M. These two talks were part of the course on Rational Design of Protein Solutions, which was also a part of PepTalk.
Rational Design of Protein Solutions:
The rational design of protein solutions combines elements of colloidal chemistry, which treats proteins as a dispersed phase, with molecular chemistry, which treats the proteins as molecules. This workshop will discuss the distinctions between the colloidal and molecular properties of protein solutions, what measurements are relevant to each, and how the solvent properties can be manipulated to provide a stable, high-concentration solution.
Overview on Colloidal Versus Molecular Solution Stability
Thomas M. Laue, Ph.D., Professor, Biochemistry and Molecular Biology; Director, Biomolecular Interaction Technologies Center (BITC), University of New Hampshire
Tom Laue is the Capenter Professor of Molecular, Cellular and Biomedical Sciences, and professor of Material Sciences at the University of New Hampshire. He is the Director of both the Center to Advance Molecular Interaction Science and the Biomolecular Interaction Technologies Center.
He received his bachelor’s degree in Natural Sciences from the Johns Hopkins University in 1971and his Ph.D. in Biophysics and Biochemistry from the University of Connecticut in 1981. His post-doctoral studies were conducted at the University of Oklahoma. Between 1969 and 1975, he worked as a technician in the deep space program of NASA.
He joined the University of New Hampshire in 1984 as an Assistant Professor, and teaches both undergraduate and graduate courses in biochemistry and biophysics. His research focuses on the development of instrumentation and methods that use the fundamental properties of mass and charge for examining macromolecular interactions. His instruments can provide unique insights into these interactions, which has resulted in extensive collaborations with both academic and industrial labs. Tom has over 120 publications, serves on several editorial boards, and gives over one hundred lectures, seminars and workshops a year.
Increasing Protein Stability and Solubility
C. Nick Pace, Ph.D., Professor, Medical Biochemistry and Genetics and of Biochemistry and Biophysics, Texas A&M
Dr. Nick Pace received his B.S. in Chemistry from the University of Utah in 1962, and his Ph.D. in Biochemistry from Duke University in 1966 working with Dr. Charles Tanford. His postdoctoral work was in the Chemistry Dept. at Cornell University working with Dr. Gordon Hammes. He joined the faculty at Texas A&M in 1968. In 1982 he took a Sabbatical at the MRC Centre in Cambridge England working with Dr. Tom Creighton and Dr. Alan Barrett. In 1992 he was a Visiting Professor at Osaka University in the Institute for Protein Research.
The important tasks in living cells are carried out by proteins in which the polypeptide chain is folded into a globular structure that is essential for their biological function. The amino acid sequence of the protein determines the folded structure. Proteins can now be constructed with any desired amino acid sequence. The potential applications of this technology in health and other areas are limited only by our knowledge and imagination. We try to learn how changes in the amino acid sequence effect the structure, function, solubility, and stability of a protein. Our ultimate goal is to be able to predict the folded structure of a protein given just the amino acid sequence.
About the Conference:
CHI’s 10th Annual PepTalk event features strong scientific programming comprising fourteen conferences within topic focused pipelines. The four distinct pipelines range from applying protein discovery research, to developing downstream protein expression, characterization, formulation, and production that ultimately leads to clinical applications. This event is designed with you in mind. Stay within a specific pipeline or track hop, and create a custom agenda to meet your research and networking needs.