Stabilization of Therapeutic Proteins
We present results of molecular simulations, quantum mechanical calculations, and experimental data aimed towards the rational design of solvent formulations. In particular, we have found that the rate limitation of oxidation of methionine groups is determined by the breaking of O-O bonds in hydroge...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | en_US |
| Published: |
2003
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| Subjects: | |
| Online Access: | http://hdl.handle.net/1721.1/3794 |
| _version_ | 1826199717826002944 |
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| author | Chu, Jhih-Wei Yin, Jin Mazyar, Oleg Goh, Lin-Tang Yap, Miranda G.S. Wang, Daniel I.C. Trout, Bernhardt L. |
| author_facet | Chu, Jhih-Wei Yin, Jin Mazyar, Oleg Goh, Lin-Tang Yap, Miranda G.S. Wang, Daniel I.C. Trout, Bernhardt L. |
| author_sort | Chu, Jhih-Wei |
| collection | MIT |
| description | We present results of molecular simulations, quantum mechanical calculations, and experimental data aimed towards the rational design of solvent formulations. In particular, we have found that the rate limitation of oxidation of methionine groups is determined by the breaking of O-O bonds in hydrogen peroxide, not by the rate of acidic catalysis as previously thought. We have used this understanding to design molecular level parameters which are correlated to experimental data. Rate data has been determined both for G-CSF and for hPTH(1-34). |
| first_indexed | 2024-09-23T11:24:36Z |
| format | Article |
| id | mit-1721.1/3794 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T11:24:36Z |
| publishDate | 2003 |
| record_format | dspace |
| spelling | mit-1721.1/37942019-04-12T08:15:24Z Stabilization of Therapeutic Proteins Chu, Jhih-Wei Yin, Jin Mazyar, Oleg Goh, Lin-Tang Yap, Miranda G.S. Wang, Daniel I.C. Trout, Bernhardt L. protein stabilization excipients molecular simulations kinetics We present results of molecular simulations, quantum mechanical calculations, and experimental data aimed towards the rational design of solvent formulations. In particular, we have found that the rate limitation of oxidation of methionine groups is determined by the breaking of O-O bonds in hydrogen peroxide, not by the rate of acidic catalysis as previously thought. We have used this understanding to design molecular level parameters which are correlated to experimental data. Rate data has been determined both for G-CSF and for hPTH(1-34). Singapore-MIT Alliance (SMA) 2003-12-08T16:17:14Z 2003-12-08T16:17:14Z 2003-01 Article http://hdl.handle.net/1721.1/3794 en_US Molecular Engineering of Biological and Chemical Systems (MEBCS); 1694999 bytes application/pdf application/pdf |
| spellingShingle | protein stabilization excipients molecular simulations kinetics Chu, Jhih-Wei Yin, Jin Mazyar, Oleg Goh, Lin-Tang Yap, Miranda G.S. Wang, Daniel I.C. Trout, Bernhardt L. Stabilization of Therapeutic Proteins |
| title | Stabilization of Therapeutic Proteins |
| title_full | Stabilization of Therapeutic Proteins |
| title_fullStr | Stabilization of Therapeutic Proteins |
| title_full_unstemmed | Stabilization of Therapeutic Proteins |
| title_short | Stabilization of Therapeutic Proteins |
| title_sort | stabilization of therapeutic proteins |
| topic | protein stabilization excipients molecular simulations kinetics |
| url | http://hdl.handle.net/1721.1/3794 |
| work_keys_str_mv | AT chujhihwei stabilizationoftherapeuticproteins AT yinjin stabilizationoftherapeuticproteins AT mazyaroleg stabilizationoftherapeuticproteins AT gohlintang stabilizationoftherapeuticproteins AT yapmirandags stabilizationoftherapeuticproteins AT wangdanielic stabilizationoftherapeuticproteins AT troutbernhardtl stabilizationoftherapeuticproteins |