Rapid measurement of inhibitor binding kinetics by isothermal titration calorimetry
There is growing evidence that the kinetics of interactions between inhibitors and their targets can strongly impact therapeutic efficacy. Here the authors describe an isothermal titration calorimetry-based method that can rapidly quantify inhibition kinetics and measure sub-nM binding affinities.
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2018-03-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-018-03263-3 |
| _version_ | 1830403955362889728 |
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| author | Justin M. Di Trani Stephane De Cesco Rebecca O’Leary Jessica Plescia Claudia Jorge do Nascimento Nicolas Moitessier Anthony K. Mittermaier |
| author_facet | Justin M. Di Trani Stephane De Cesco Rebecca O’Leary Jessica Plescia Claudia Jorge do Nascimento Nicolas Moitessier Anthony K. Mittermaier |
| author_sort | Justin M. Di Trani |
| collection | DOAJ |
| description | There is growing evidence that the kinetics of interactions between inhibitors and their targets can strongly impact therapeutic efficacy. Here the authors describe an isothermal titration calorimetry-based method that can rapidly quantify inhibition kinetics and measure sub-nM binding affinities. |
| first_indexed | 2024-12-20T17:18:24Z |
| format | Article |
| id | doaj.art-695ef23f7e8d4d87a44cc9ad450d7ebc |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-20T17:18:24Z |
| publishDate | 2018-03-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-695ef23f7e8d4d87a44cc9ad450d7ebc2022-12-21T19:31:56ZengNature PortfolioNature Communications2041-17232018-03-01911710.1038/s41467-018-03263-3Rapid measurement of inhibitor binding kinetics by isothermal titration calorimetryJustin M. Di Trani0Stephane De Cesco1Rebecca O’Leary2Jessica Plescia3Claudia Jorge do Nascimento4Nicolas Moitessier5Anthony K. Mittermaier6Department of Chemistry, McGill UniversityDepartment of Chemistry, McGill UniversityDepartment of Chemistry, McGill UniversityDepartment of Chemistry, McGill UniversityDepartment of Chemistry, McGill UniversityDepartment of Chemistry, McGill UniversityDepartment of Chemistry, McGill UniversityThere is growing evidence that the kinetics of interactions between inhibitors and their targets can strongly impact therapeutic efficacy. Here the authors describe an isothermal titration calorimetry-based method that can rapidly quantify inhibition kinetics and measure sub-nM binding affinities.https://doi.org/10.1038/s41467-018-03263-3 |
| spellingShingle | Justin M. Di Trani Stephane De Cesco Rebecca O’Leary Jessica Plescia Claudia Jorge do Nascimento Nicolas Moitessier Anthony K. Mittermaier Rapid measurement of inhibitor binding kinetics by isothermal titration calorimetry Nature Communications |
| title | Rapid measurement of inhibitor binding kinetics by isothermal titration calorimetry |
| title_full | Rapid measurement of inhibitor binding kinetics by isothermal titration calorimetry |
| title_fullStr | Rapid measurement of inhibitor binding kinetics by isothermal titration calorimetry |
| title_full_unstemmed | Rapid measurement of inhibitor binding kinetics by isothermal titration calorimetry |
| title_short | Rapid measurement of inhibitor binding kinetics by isothermal titration calorimetry |
| title_sort | rapid measurement of inhibitor binding kinetics by isothermal titration calorimetry |
| url | https://doi.org/10.1038/s41467-018-03263-3 |
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