Decades of drug development work have taught us something important: often, the best medicines are found in nature. But nature can be improved upon. That’s where biologics research comes in. Researchers in this field are concerned with optimizing natural drug products to make them safer and more effective.
Bringing new and improved biologic therapeutics to the clinic requires in-depth stability profiling and optimization during development and formulation. Researchers profile their candidates’ stability with parameters such as melting temperature (Tm), energy of unfolding (ΔG), and sample homogeneity (polydispersity index – PDI). These stability properties are used to make decisions about which candidates are worth further investment. Read more about how NanoTemper enables biologics researchers to get high-quality stability information for profiling their candidates.
Monoclonal antibodies and antibody-derived treatments
Monoclonal antibodies (mAbs) are a staple of the biologics market. Hundreds of currently available therapies are antibody-based. When developing mAbs, their fragment derivatives (Fabs), or bi-specific Abs, it is crucial to weed out unstable candidates early in the development process.
Evaluate mAb stability early in the development process with Tm and Ton
Finding the best mAbs for development during the early discovery process requires the assessment of multiple biophysical characteristics of each candidate. Learn how this group at Merck profiles their candidates using Tm and Ton derived from nanoDSF.
Profile biosimilars with nanoDSF as a fast, high-throughput alternative to DSC
Biosimilar drugs are biologic therapeutics that are highly similar to therapeutics that have already been approved by regulatory bodies such as the FDA. They exhibit slight differences from their reference product, and it is important to ensure that they retain the stability profile after modification. Read why nanoDSF is the most effective choice for profiling biosimilars’ stability.
Increase Fab yield by measuring the free energy values of refolding
Antibody fragments (Fabs) offer expression and purification advantages compared to full-length antibodies. However, concerns remain about how to efficiently scale up the process. Refolding from inclusion bodies produced in E.Coli offers an avenue for larger yields of Fabs during production. See how one group used chemical denaturation with nanoDSF to profile the refolding potential of two commercially available Fabs.
Other therapeutic proteins
Biologics aren’t limited to mAbs and other antibody-derived proteins. Proteins such as enzymes or receptors are also considered biologics, and researchers are concerned with profiling these molecules not only for their stability but also for their ability to interact with disease-related targets in vivo.
Pave the way towards personalized vaccines with in-depth nanoDSF profiling of MHC I:peptide complexes
The particular make-up of a patient’s Major Histocompatibility Complex Class I (MHC-I) ultimately determines their ability to develop an immune response for a given antigen. See why this group established nanoDSF as the best method to profile the affinity of MHC-I to neoantigen peptides.
Avoid liabilities for biotherapeutic proteins with multi-parameter buffer assessment
Non-IgG based therapeutics have different biophysical characteristics than mAbs. While the process for formulation and development is broadly similar, there are additional considerations such as glycosylation patterns that present molecule-specific liabilities. Learn what multi-parameter assessments are required when formulating non-mAb-based biologics.
Screening and formulation
Long-term biologics stability is top-of-mind for all researchers. Any biologic candidate must demonstrate its ability to withstand scale-up, bulk manufacturing, and storage ahead of clinical administration. Performing long-term stability studies early on is essential to ensure a biologic makes it successfully to market.
Find the right buffer excipients for stabilizing therapeutic mAbs
An oft-overlooked consideration for formulation is the addition of excipients to stabilize mAbs. Read how thermal stability studies with nanoDSF efficiently screened a new set of substances to find stabilizing agents for therapeutic proteins.
Optimize formulation for target proteins as a key step for vaccine research
A major hurdle in HIV vaccine development is the production of stable antigen protein to use for assays. Researchers used the Prometheus Panta to measure the DLS and nanoDSF parameters of this vaccine antigen and determine the ideal FDA-approved buffer formulation.
Screen multiple classes of therapeutic proteins with nanoDSF
Historically, gold-standard data for melting temperatures was obtained from differential scanning calorimetry (DSC). Here, Amgen demonstrates that nanoDSF experiments enabled by the Prometheus give comparable data quality, with less sample consumption and faster throughput. See why Prometheus is truly the new gold standard in protein characterization.