Pre-Formulation and Formulation Studies

How Can Pall Life Sciences Help You With Your Pre-Formulation/Formulation Needs? Pall Corporation recently signed an exclusive commercial agreement with Avacta Group (Press Release). As part of the agreement, Avacta and Pall will collaborate to develop and market products and advanced analytical services for the life sciences market. The relationship will initiate plans to market and support Optim® system, Avacta’s market leading ultra-low volume biopharmaceutical analysis tool, in North America.

Optim 1000 System

The Optim 1000 system is designed to enable the identification of candidate molecules or formulations with the most favorable properties much earlier in the development process, thereby eliminating the candidates or formulations that do not have the potential of manufacturability. 

The Optim1000 system is ideal for:

• Candidate screening
• Optimizing formulation parameters
• Determining the effects of process holds and elution conditions as part of process optimization 
• Measuring protein stability during freeze-thaw cycles, mechanical stress testing and other forced stability trials

For more information or to learn how the Optim 1000 system can help you accelerate your formulation studies and economize drug development processes, Contact Pall.

Learn more about the Optim1000 system:

• Brochure - Optim 1000: A truly unique high throughput, micro-volume protein analysis and characterisation system
• Frequently asked questions about the performance and capability of the Optim 1000
• Avacta Optim 1000 Business Case
• Application Note - Optim 1000: Characterization of Protein Structural Stability
• Application Note - Optim 1000: Characterization of Protein Aggregation
• Application Note - Optim 1000: Preformulation of a Biopharmaceutical Using Optim
• Technical Note - Optim 1000: Fluorescence data analysis methods
• Technical Note - Optim 1000: Comparison of Optim with Standard Methods to Determine Thermal Unfolding Midpoint, T_m
• Technical Note - Optim 1000: An Introduction to Proteins, Their Folding and Aggregation

Why are Formulation, Stability, Comparability and Characterization Important?

Proteins are complex and sensitive molecules held together by weak physical forces such as hydrophobic and electrostatic interactions and disulfide bonds. A protein’s native three-dimensional structural conformation determines long-term stability and biological potency. A number of factors such as changes in pH, temperature, types of buffers, excipients, high sheer, aggregation, etc. can have a disruptive effect on this structural conformation and affect stability and solubility of the protein. Change in a protein's structure can lead to aggregation resulting in immunogenicity, negatively impacting its therapeutic effect.

Successful pre-formulation research leads to identification of potential protein degradation pathways and development of robust buffer and formulation pH and excipient selection. The protein stability data under a range of solution conditions becomes valuable in purification and process development as well.

As a biopharmaceutical product moves into clinical manufacturing, collection of stability data and demonstration of comparability following scale up, a manufacturing site change, and during process validation become critical. These data are used to support formulation development to determine protein concentration, presence of additives, pH, temperature of storage, type of container, and exposure to light, air and humidity, all of which can affect packaging, storage, shipping and handling, until the ultimate delivery to the target site in the patient.