Biophysical Characterization and Analysis
A diversity of conventional analytical methods such as UV-Vis spectroscopy and LC-MS can be used to support the early stages of biologics development. Nowadays, more and more techniques have become available to better characterize drug substances. BOC Sciences has developed an appropriate methodology to study the key biophysical and chemical properties of biological drug substances. For complex molecules such as proteins, antibodies or various conjugates, our team has established a series of orthogonal methods to determine most properties of a drug substance or drug product. Our well-designed platform is equipped with state-of-the-art equipment and analytical methods for the biophysical characterization and analysis of proteins, including higher-order structure characterization, monomer/aggregate species determination, free sulfhydryl content determination and thermal stability characterization.
Figure 1. Genetic constructions from Thermotoga maritima. (Mcconnell, A. D.; Spasojevich, V. et al.2012)
Our Services
To make it easier and better for researchers, BOC Sciences provides biophysical characterization and analysis service in a competitive fashion. We have provided a more efficient way to increase the number of new drugs, greatly shorten the R&D cycle, and reduce the development costs.
- Structural characterization
We offer a comprehensive range of analytical techniques to determine or confirm the solid state molecular structure of your biologics. Our scientific expertise is combined with unique analysis equipment to help characterize your material and guide your compound development. At BOC Sciences, mass spectrometry, NMR spectroscopy, IR spectroscopy, elemental analysis, single crystal X-ray diffraction, thermal analysis and calorimetry are available
- Thermal analysis and calorimetry
We monitor thermochemical events and weight loss as a function of temperature to achieve insight into solid form characteristics, polymorphic transformation mechanisms, and solid state degradation pathways. Our teams provide reliable thermogravimetric analysis and differential scanning calorimetry data
- Unknown particle identification
Our experienced experts can identify and mitigate contamination in your product's manufacturing process, helping our customers avoid manufacturing inefficiencies, compromised product quality, and delays in getting product where it needs to go. We use microscopic and spectroscopic techniques to rapidly characterize contaminants to provide important data
- Aggregation biophysical studies
We apply Differential scanning calorimetry, analytical ultracentrifugation, and light scattering techniques to study the non-covalent structural aspects of a protein, and aggregates or oligomer formation in solution
- Protein and peptide crystallization
Our expert scientists offer crystallization screening services using a variety of crystallization techniques. In addition, we use these crystallization techniques for single crystal growth of proteins and peptides for 3-D structure determination
Figure 2. Fluorescence excitation and emission spectra. (Mcconnell, A. D.; Spasojevich, V. et al.2012)
Biophysical Characterization and Analysis Technologies
- Mass Spectrometry: Accurate identification of proteins, peptides, oligonucleotides, PEGylated proteins, ADCs and other polymers in extremely small quantities, de novo peptide sequencing and identification of modified sites, and accurate determination of drug-to-antibody ratio and drug load distribution of ADCs
- NMR Spectroscopy: Determination of the 3-D structures of proteins, peptides and oligonucleotides, Liquid and solid state analysis, and identification and structure determination
- Fourier Transform Infrared Spectroscopy (FTIR): Quantification of different secondary structural elements
- Intrinsic fluorescence: Determination of the tertiary structure of a protein
- Circular Dichroism (CD): Higher order structure characterization
- Infrared Spectroscopy (IRS): Characterization of protein secondary structures
- Size Exclusion-Multi-Angle Light Scattering (SEC-MALS): Determination of protein monomer and aggregates molecular weight
- Analytical Ultracentrifuge (AUC): Determination of protein molecular weight and aggregation states in native solution
- Amino Acid Concentration Analysis (AAA): Determination of concentration of amino acids in cell culture medium or after protein/peptide hydrolysis
- Determination of Extinction Coefficient (EC): Determination of concentration of amino acids in cell culture medium or after protein/peptide hydrolysis
- Determination of Free Sulfhydryl (Free-SH) Content
- Dynamic Light Scattering (DLS): Determination of particle sizes, PDI and Zeta-potential of proteins
- Differential Scanning Calorimeter (DSC): Characterization of protein thermal stability
Figure 3. TEM images show their self-assembly into spherical nanocompartments. (Mcconnell, A. D.; Spasojevich, V. et al.2012)
Why choose BOC Sciences?
Our dedicated CMC team has provided tailored solutions to our clients from engagement to launch. With many years of industry experience, we provide clients with the following:
- Comprehensive, integrated CMC services with a flexible service model that grows with your programs
- Knowledgeable industry experts who deliver scalable, actionable insights
- World-class facilities and equipment that remain at the forefront of the global pharmaceutical research, analytical and development standards
- Our comprehensive services support products at every stage of the product lifecycle, from early-stage discovery to full commercial cGMP manufacture
- A focus on risk management that is designed to ensure completion of your technical goals
BOC Sciences provides professional, rapid and high-quality services of biophysical characterization and analysis at competitive prices for global customers. Personalized and customized services of biophysical characterization and analysis can satisfy any innovative scientific study demands. Our clients have direct access to our staff and prompt feedback to their inquiries. If you are interested in our services, please contact us immediately!
Reference
- Mcconnell, A. D.; Spasojevich, V. et al. An integrated approach to extreme thermostabilization and affinity maturation of an antibody. Protein Engineering Design and Selection. 2012. 26(2): 151-163.
