| 00:00:00 | The Combination of Dynamic Light Scattering and Raman Spectroscopy for the Analysis of Protein Structure and Stability |
| 00:01:13 | Protein Aggregation and Stability |
| 00:01:31 | Untitled |
| 00:02:17 | Untitled |
| 00:02:58 | Untitled |
| 00:03:18 | Untitled |
| 00:03:59 | Untitled |
| 00:04:41 | Untitled |
| 00:05:22 | Untitled |
| 00:05:52 | Zetasizer Helix: Raman Spectra of a mAb |
| 00:07:25 | Zetasizer Helix: Data Acquisition Modes |
| 00:08:17 | Zetasizer Helix: Data Analysis Software |
| 00:09:25 | Application Areas |
| 00:10:48 | Case Study: Comparing the Thermal Stability and Aggregation Kinetics of a Biosimilar Formulation to the Innovator Product |
| 00:11:08 | Comparing the Thermal Stability and Aggregation Kinetics of a Biosimilar Formulation to the Innovator Product |
| 00:12:20 | Comparison of mAb A Formulation and mAb B Formulation at 20 °C |
| 00:12:33 | Comparing Spectral Data from mAb A and mAb B at 20 °C |
| 00:12:59 | Untitled |
| 00:13:38 | Untitled |
| 00:13:46 | Comparing DLS Data from mAb A and mAb B at 20 °C |
| 00:14:14 | Untitled |
| 00:14:51 | Thermal Ramp Measurements: Evaluating Thermal Stability at Formulation Conditions |
| 00:15:01 | Thermal Stability Measurement of mAb ASize and Conformation |
| 00:15:56 | Untitled |
| 00:16:44 | Untitled |
| 00:16:59 | Untitled |
| 00:17:41 | Untitled |
| 00:18:26 | Untitled |
| 00:18:42 | Thermal Stability Summary and Comparison of mAb A and mAb B |
| 00:20:26 | Untitled |
| 00:21:12 | Isothermal Incubation Measurements: Correlating Aggregation Kinetics and Structural Change |
| 00:21:41 | Isotherm Incubation Studies Near Melting/Transition Temperature |
| 00:23:08 | Untitled |
| 00:24:10 | Isotherm Incubation Studies Near Melting/Transition Temperature |
| 00:25:36 | Isotherm Incubation Studies Near Melting/Transition Temperature |
| 00:27:29 | Isotherm Incubation Studies Near Melting/Transition Temperature |
| 00:29:10 | Isothermal Incubation Summary and Conclusions |
| 00:30:13 | Case Study Summary |
| 00:30:39 | Untitled |
| 00:30:50 | Thank you for your attentionAny questions? |
| 00:31:02 | Isotherm Incubation Studies Near Melting/Transition Temperature |
| 00:31:55 | Thank you for your attentionAny questions? |
| 00:32:34 | Untitled |
| 00:34:02 | Thank you for your attentionAny questions? |
| 00:35:11 | Contact Information |
There are many technologies available for the increased understanding of protein unfolding and stability, including calorimetry, spectroscopy, and light scattering techniques. In recent years, Raman spectroscopy has proven to be useful for the characterization of protein therapeutics, with its ability to monitor protein conformation via multiple secondary and tertiary structural markers acquired from a single measurement.
Additionally, Raman spectroscopy is perfectly suited for studying high concentration protein samples (as high as 150 mg/mL) with minimal, if any, sample preparation. By combining dynamic light scattering (DLS) and Raman spectroscopy onto a single platform, information about protein hydrodynamic size distributions and conformational changes can be obtained from a single sample under formulation conditions, leading to increased understanding of protein aggregation and unfolding pathways.
This webinar will introduce the combined platform of DLS and Raman spectroscopy and provide a case study of biotherapeutic relevance.
Additionally, Raman spectroscopy is perfectly suited for studying high concentration protein samples (as high as 150 mg/mL) with minimal, if any, sample preparation. By combining dynamic light scattering (DLS) and Raman spectroscopy onto a single platform, information about protein hydrodynamic size distributions and conformational changes can be obtained from a single sample under formulation conditions, leading to increased understanding of protein aggregation and unfolding pathways.
This webinar will introduce the combined platform of DLS and Raman spectroscopy and provide a case study of biotherapeutic relevance.