Nano Differential Scanning Fluorimetry-Based Thermal Stability Screening and Optimal Buffer Selection for Immunoglobulin G
Nano differential scanning fluorimetry (nanoDSF) is a high-throughput protein stability screening technique that simultaneously monitors protein unfolding and aggregation properties. The thermal stability of immunoglobulin G (IgG) was investigated in three different buffers (sodium acetate, sodium c...
| Main Authors: | , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2021-12-01
|
| Series: | Pharmaceuticals |
| Subjects: | |
| Online Access: | https://www.mdpi.com/1424-8247/15/1/29 |
| _version_ | 1797491261335142400 |
|---|---|
| author | Soo Hyun Kim Han Ju Yoo Eun Ji Park Dong Hee Na |
| author_facet | Soo Hyun Kim Han Ju Yoo Eun Ji Park Dong Hee Na |
| author_sort | Soo Hyun Kim |
| collection | DOAJ |
| description | Nano differential scanning fluorimetry (nanoDSF) is a high-throughput protein stability screening technique that simultaneously monitors protein unfolding and aggregation properties. The thermal stability of immunoglobulin G (IgG) was investigated in three different buffers (sodium acetate, sodium citrate, and sodium phosphate) ranging from pH 4 to 8. In all three buffers, the midpoint temperature of thermal unfolding (<i>T</i><sub>m</sub>) showed a tendency to increase as the pH increased, but the aggregation propensity was different depending on the buffer species. The best stability against aggregation was obtained in the sodium acetate buffers below pH 4.6. On the other hand, IgG in the sodium citrate buffer had higher aggregation and viscosity than in the sodium acetate buffer at the same pH. Difference of aggregation between acetate and citrate buffers at the same pH could be explained by a protein–protein interaction study, performed with dynamic light scattering, which suggested that intermolecular interaction is attractive in citrate buffer but repulsive in acetate buffer. In conclusion, this study indicates that the sodium acetate buffer at pH 4.6 is suitable for IgG formulation, and the nanoDSF method is a powerful tool for thermal stability screening and optimal buffer selection in antibody formulations. |
| first_indexed | 2024-03-10T00:44:55Z |
| format | Article |
| id | doaj.art-38bb91043f8a42a2bc7e4b008711aee0 |
| institution | Directory Open Access Journal |
| issn | 1424-8247 |
| language | English |
| last_indexed | 2024-03-10T00:44:55Z |
| publishDate | 2021-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Pharmaceuticals |
| spelling | doaj.art-38bb91043f8a42a2bc7e4b008711aee02023-11-23T15:00:59ZengMDPI AGPharmaceuticals1424-82472021-12-011512910.3390/ph15010029Nano Differential Scanning Fluorimetry-Based Thermal Stability Screening and Optimal Buffer Selection for Immunoglobulin GSoo Hyun Kim0Han Ju Yoo1Eun Ji Park2Dong Hee Na3Department of Pharmacy, College of Pharmacy, Chung-Ang University, Seoul 06974, KoreaDepartment of Pharmacy, College of Pharmacy, Chung-Ang University, Seoul 06974, KoreaD&D Pharmatech, Seongnam 13486, KoreaDepartment of Pharmacy, College of Pharmacy, Chung-Ang University, Seoul 06974, KoreaNano differential scanning fluorimetry (nanoDSF) is a high-throughput protein stability screening technique that simultaneously monitors protein unfolding and aggregation properties. The thermal stability of immunoglobulin G (IgG) was investigated in three different buffers (sodium acetate, sodium citrate, and sodium phosphate) ranging from pH 4 to 8. In all three buffers, the midpoint temperature of thermal unfolding (<i>T</i><sub>m</sub>) showed a tendency to increase as the pH increased, but the aggregation propensity was different depending on the buffer species. The best stability against aggregation was obtained in the sodium acetate buffers below pH 4.6. On the other hand, IgG in the sodium citrate buffer had higher aggregation and viscosity than in the sodium acetate buffer at the same pH. Difference of aggregation between acetate and citrate buffers at the same pH could be explained by a protein–protein interaction study, performed with dynamic light scattering, which suggested that intermolecular interaction is attractive in citrate buffer but repulsive in acetate buffer. In conclusion, this study indicates that the sodium acetate buffer at pH 4.6 is suitable for IgG formulation, and the nanoDSF method is a powerful tool for thermal stability screening and optimal buffer selection in antibody formulations.https://www.mdpi.com/1424-8247/15/1/29nano differential scanning fluorimetryimmunoglobulin Gstabilityaggregationantibody formulation |
| spellingShingle | Soo Hyun Kim Han Ju Yoo Eun Ji Park Dong Hee Na Nano Differential Scanning Fluorimetry-Based Thermal Stability Screening and Optimal Buffer Selection for Immunoglobulin G Pharmaceuticals nano differential scanning fluorimetry immunoglobulin G stability aggregation antibody formulation |
| title | Nano Differential Scanning Fluorimetry-Based Thermal Stability Screening and Optimal Buffer Selection for Immunoglobulin G |
| title_full | Nano Differential Scanning Fluorimetry-Based Thermal Stability Screening and Optimal Buffer Selection for Immunoglobulin G |
| title_fullStr | Nano Differential Scanning Fluorimetry-Based Thermal Stability Screening and Optimal Buffer Selection for Immunoglobulin G |
| title_full_unstemmed | Nano Differential Scanning Fluorimetry-Based Thermal Stability Screening and Optimal Buffer Selection for Immunoglobulin G |
| title_short | Nano Differential Scanning Fluorimetry-Based Thermal Stability Screening and Optimal Buffer Selection for Immunoglobulin G |
| title_sort | nano differential scanning fluorimetry based thermal stability screening and optimal buffer selection for immunoglobulin g |
| topic | nano differential scanning fluorimetry immunoglobulin G stability aggregation antibody formulation |
| url | https://www.mdpi.com/1424-8247/15/1/29 |
| work_keys_str_mv | AT soohyunkim nanodifferentialscanningfluorimetrybasedthermalstabilityscreeningandoptimalbufferselectionforimmunoglobuling AT hanjuyoo nanodifferentialscanningfluorimetrybasedthermalstabilityscreeningandoptimalbufferselectionforimmunoglobuling AT eunjipark nanodifferentialscanningfluorimetrybasedthermalstabilityscreeningandoptimalbufferselectionforimmunoglobuling AT dongheena nanodifferentialscanningfluorimetrybasedthermalstabilityscreeningandoptimalbufferselectionforimmunoglobuling |