Our Services for Protein Biophysics and Peptide Biophysics
Protein protein interactions and protein peptide interactions are the backbone of almost every vital cellular process, ranging from DNA replication and transcription, over protein biosynthesis and degradation, to signal response, cell-cell communication, and immune defense. Studying and modifying protein protein interactions and protein peptide interactions is thus key for many therapeutic and diagnostic applications.
We have thus developed a portfolio of tailor-made protein biophysics services that allow for the precise, robust, fast, and cost-efficient analysis of almost any type of protein protein interaction, protein peptide interaction or protein binding to various targets with MST, nanoDSF, BLI, and ITC. Moreover, we are able to analyze protein stability, thermal protein unfolding, chemical protein unfolding, protein denaturation, and protein aggregation using the state-of-the-art, label-free, in-solution nanoDSF method.
If you are interested in specific example applications, please have a look at our application notes. You can also use the contact form below to ask us anything about the services outlined below. We will get back to you shortly with a solution made specifically for your request!
Assays for Protein Protein Interactions and Protein Binding
Precise information about the interaction of a protein or a peptide either with its natural ligands (e.g. receptor-ligand interaction) or with a variety of other types of targets is key for understanding the functional role of these molecules in a cell. Just the same, understanding protein protein interaction and protein binding to natural ligands or artificial inhibitors and drugs is paramount for developing synthetic and therapeutic ligands as well as for utilizing these molecules for diagnostic purposes.
Steady-state Protein Binding Assay - MST
Determine the steady-state affinity (KD) of your protein or peptide to its natural ligand or to other possible targets, including ions, small molecules, peptides, DNA, RNA, proteins, or synthetic particles.
Kinetic Protein Binding Assay - BLI
Study on- and off-rates (kon, koff) of interactions between proteins or peptides and their ligands or target. Compare different protein preparations with respect to their kinetic behavior.
Thermodynamic Protein Binding Assay - ITC
Characterize protein-target or peptide-target interactions with respect to their thermodynamic parameters, including enthalpy (ΔH), free enthalpy of binding (ΔG), entropy (ΔS), and stoichiometry.
Assays in Biological Liquids - MST
Determine protein-protein interactions in relevant biological liquids such as serum, plasma, cell lysate, urine, mucose, or environmental matrices. Exclude unwanted side-interactions in these biological matrices.
Competition Assay - MST, BLI
Determine the ability of your protein or peptide to disrupt the complex of a target molecule and its natural ligand. Alternatively, test the influence of the protein/peptide on interactions between a target and its ligand.
Studying Protein Stability and Protein Unfolding
Information about thermal protein stability is essential in many cases. For example, high protein stability is an important factor for mutational scanning of a protein. Also, therapeutic and diagnostic applications often require proteins to be very stable under the most diverse conditions.
Our precise, versatile, fast, and cost-efficient nanoDSF platform allows for the determination of protein stability in a wide range of applications outlined below. Moreover, nanoDSF allows for the label-free, in-solution analysis of thermal and chemical protein unfolding as well as the detection of protein denaturation and protein aggregation. Importantly, no extrinsic fluorescent dye like in traditional DSF methods is required.
Protein Stability Buffer Screening
Find the optimal buffer or buffer additives for your protein in a pre-formulation phase buffer screening. We hold ready up to 500 buffers specifically selected from FDA-approved formulations.
Long-term Storage Optimization
Identify the optimal conditions for storing your protein over a defined period of time. Long-term storage assays can be added as a subsequent module after buffer screening assays.
Test the stability of your antibody under different stress conditions. For example, chemically induced unfolding, freeze-thaw cycling, thermal stress, as well as mechanical stress.
Protein Stability/Protein Unfolding Batch comparison
Compare different batches of your protein of interest with respect to its thermal stability and thermal unfolding behavior. These assays can be easily combined with buffer screening and long-term stability tests.