How “fingerprinting” vaccine candidates saves time
Vaccine development is now more rapid than ever before, and we’re all working towards a common goal: decreasing the time it takes to bring vaccines to the people who need them. In this three-part blog series, we show how differential scanning calorimetry (DSC) can help you speed up vaccine candidate selection. In our first blog, we’ll begin by addressing the importance of a vaccine candidate’s ‘fingerprint’.
Fingerprinting vaccine candidate structures
Vaccine candidate structures are like snowflakes: unique (and best kept cold). Each higher-order structure of a vaccine candidate has a ‘fingerprint’. This fingerprint is critical for product characterization, formulation development and comparability analyses. As developers continue looking into new candidates, these areas become more and more important.
Protein subunit vaccines
Protein subunit vaccines are well investigated, and work on a wide range of diseases like Hepatitis B, tetanus, and typhoid. We must characterize these subunits, so unstable candidates can be identified and screened out early in the development process. This saves both time and money in the long run, by only investigating promising vaccine candidates.
However, as protein subunit vaccines continue to evolve, we need to create the most effective antigen combination from increasingly complex structural molecules. And it’s tricky.
Overcoming the challenges of mRNA vaccines
While protein subunit vaccines remain a popular choice, new technologies are emerging. mRNA and adenovirus vector vaccines have broken through to the market in a BIG way. But vaccines like these present a new set of challenges.
mRNA vaccines are composed of biomolecular assemblies. Sub-strains of the same virus can have very different structures, causing variations in vaccine stability in viral vector and virus-like particle candidates. This means that any changes in the production processes can generate a range of mRNA-lipid assemblies of varying sizes and structures.
This variability can delay development if you’re not able to choose your optimal strain or assembly from the start. And it can be expensive too.
Speeding up development with better data
We don’t need to tell you how important, lengthy and expensive clinical trials are when it comes to developing a new vaccine. Speeding the process up, without cutting corners, helps get vaccines to those who need them more quickly.
So how do you achieve this? Having a robust quality-by-design (QbD)-based program enables you to ‘home-in’ on candidates that are most likely to perform well in clinical trials. This means gathering as much information as possible about the protein structure of the vaccine candidates.
So, what information helps with vaccine development? When working with viral-vector and virus-like particles, you need a detailed understanding of the protein structure of the particle or virus capsid.
Protein structure directly impacts the stability of the resulting vaccine in different environmental conditions or formulations. When you understand and optimize protein stability early on in vaccine development, you increase the likelihood of a successful clinical trial.
DSC and fingerprinting
MicroCal PEAQ-DSC microcalorimeters can be used to determine stability and characterization data for proteins, providing that valuable fingerprint. Even better, this can be extended to all biomolecules – including the mRNA-lipid assemblies that are so important in mRNA vaccine development.
More specifically, MicroCal PEAQ-DSC measures the thermal stability of a protein, a critical parameter that will determine the stability of the protein and its unique fingerprint. Once we have this information, we can get on with narrowing down our candidates.
So, we’re beginning to see how DSC helps optimize the process so researchers can choose the best vaccine candidates quickly. In the next blog of this series, we’ll show you how exactly DSC works.
Download the full guide here to find out how DSC can improve your vaccine development program.