During the development and production of modern therapeutics—encompassing both biological and non-biological complex drugs—various analytical challenges arise. It is essential to achieve accurate, rapid, and rigorous quantitative results to successfully deliver these products to patients.
The Waters, Wyatt Technologies, and TA Instruments portfolio offers a comprehensive range of systems, solutions, and support to enhance your capability in obtaining detailed biophysical characterization throughout the development cycle. From discovery and cell line development to formulation and quality control, Waters has you covered.
eBook: Characterization of Biologics and Complex Drugs
While developing and producing modern therapeutics—both biological and non-biological complex drugs—numerous analytical challenges emerge. Obtaining quantitative results accurately, rapidly, and rigorously is crucial for successfully bringing these products to patients.
Explore our end-to-end solutions for advanced characterization of antibodies and protein-based therapies, vaccines, gene therapies, nanomedicines, peptides, and nucleic acids.
While developing and producing modern therapeutics—both biological and non-biological complex drugs—numerous analytical challenges emerge. Obtaining quantitative results accurately, rapidly, and rigorously is crucial for successfully bringing these products to patients.
Explore our end-to-end solutions for advanced characterization of antibodies and protein-based therapies, vaccines, gene therapies, nanomedicines, peptides, and nucleic acids.
Measure a wide variety of molecular interactions with the Affinity ITC, designed for the most challenging life science applications that require high sensitivity and high productivity for the highest quality isothermal titration calorimetry (ITC) data.
Quantify the thermal stability of large biomolecules and biotherapeutics with the Nano DSC that quickly measures the heat of reaction from tertiary and secondary structure changes occurring when a biomolecule unfolds or melts in nucleic acids and lipids.
The TA Instruments RS-DSC (Rapid Screening-Differential Scanning Calorimeter) is a powerful instrument that revolutionizes the thermal stability testing of high-concentration biologic drugs with its high efficiency and streamlined analysis.
The DSC 2500 with Modulated DSC and patented T4P Tzero heat flow delivers the highest sensitivity and resolution to obtain accurate results every time for your lyophilization optimization needs.
Understand the flow properties of your biologic formulations with the HR 20 for injectability and fill and finish applications for more than just viscosity.
The DAWN MALS detector assists at every development stage. Couple with Eclipse to measure binding affinity during discovery. Place downstream of any LC and perform advance analysis of biosimilar protein-conjugate ratio, post-translational modifications, and aggregation.
The DynaPro ZetaStar instrument combines DLS, SLS, and ELS in one platform. Designed for biopharma in mind, it can measure zeta-potential in formulation buffer without dilution.
Measure size, polydispersity, and Tagg data for hundreds of samples with as little as 4 µL per well. The DynaPro DLS Plate Reader uses standard-well plates and integrates with any liquid handler to further boost productivity.
ultraDAWN directly monitors titer, size, and impurities in real-time. It connects downstream purification and enrichment methods, such as IEX, FPLC, or TFF.
Gain improvements in separation and detection of metal-sensitive analytes with the ACQUITY Premier System featuring MaxPeak High Performance Surfaces (HPS) Technology, enabling you to minimize the risk of undetected analytes.
Characterize aggregates and fragments with SEC-MALS. Aided by the superb separation power of UPLC, SEC-MALS identifies and quantifies the peaks observed for a degraded mAb, in terms of molecular weight and total eluting mass. Fragments such as dual and single heavy chains, and small oligomers such as dimers consisting of monomer + fragments, are found.
An ITC experiment can rapidly quantify the exothermic or endothermic non-covalent binding of two proteins. When two proteins interact and bind, conformational changes in the proteins, and rearrangement of the solvent in the vicinity of the binding site, result in the absorption or generation of heat. Quantification of this reaction heat by ITC provides a complete thermodynamic description of the binding interaction, the stoichiometry of binding, and the association constant; in addition, if structural information is available, the contributions of specific amino acids mediating the binding event can be identified and their thermodynamic contributions quantified.
Antibody DSC Thermogram. Deconvolute each domain with typical unfolding as follows: CH2, Fab, CH3.
Overlay of replicate data from screening of Herceptin Trastuzumab in histidine, borate, PBS, and succinate buffer. Data collected in triplicate at an antibody concentration of ~20 mg/mL with a scan rate of 1 °C/min. Identify which buffers to move forward with in development by looking at Tonset and TM.
Modulated DSC (MDSC) data for 40% sucrose/water solution. Identify the glass transition for lyophilization in complex samples by separating out the reversible (heat capacity) and irreversible (kinetic events) heat signals.
HT-DLS provides more sizing and aggregation data, on more samples and more formulations with far less effort.
XBridge Protein SEC 250 Å, 2.5 µm particles were packed into both hydrophilic MaxPeak High Performance Surfaces hardware (left) and conventional stainless steel hardware (right) to clearly demonstrate the benefit afforded by the HPS hardware. Excellent monomer peak shape and HMWS recovery for NISTmAb (RM 8671) was achieved with the hydrophilic MaxPeak HPS Column, even at low NaCl concentrations.
