Low-Transition-Temperature Mixtures (LTTMs) for Dissolving Proteins and for Drug Formulation

Several diverse proteins are found to readily dissolve in neat low-transition-temperature mixtures (LTTMs). They undergo no irreversible denaturation in such unusual solvents, and the resistance of hen egg-white lysozyme against thermoinactivation in LTTMs is greater than in aqueous solution at extr...

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Main Authors: Su, Erzheng, Klibanov, Alexander M.
Other Authors: Massachusetts Institute of Technology. Department of Biological Engineering
Format: Article
Language:English
Published: Springer US 2016
Online Access:http://hdl.handle.net/1721.1/103634
https://orcid.org/0000-0003-3830-714X
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author Su, Erzheng
Klibanov, Alexander M.
author2 Massachusetts Institute of Technology. Department of Biological Engineering
author_facet Massachusetts Institute of Technology. Department of Biological Engineering
Su, Erzheng
Klibanov, Alexander M.
author_sort Su, Erzheng
collection MIT
description Several diverse proteins are found to readily dissolve in neat low-transition-temperature mixtures (LTTMs). They undergo no irreversible denaturation in such unusual solvents, and the resistance of hen egg-white lysozyme against thermoinactivation in LTTMs is greater than in aqueous solution at extreme pHs. Separately, the water-sensitive drug aspirin is found to form concentrated transparent LTTMs, where it is some 10-fold more stable against cleavage than in water.
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spelling mit-1721.1/1036342022-09-29T20:23:06Z Low-Transition-Temperature Mixtures (LTTMs) for Dissolving Proteins and for Drug Formulation Su, Erzheng Klibanov, Alexander M. Massachusetts Institute of Technology. Department of Biological Engineering Massachusetts Institute of Technology. Department of Chemistry Klibanov, Alexander M. Su, Erzheng Several diverse proteins are found to readily dissolve in neat low-transition-temperature mixtures (LTTMs). They undergo no irreversible denaturation in such unusual solvents, and the resistance of hen egg-white lysozyme against thermoinactivation in LTTMs is greater than in aqueous solution at extreme pHs. Separately, the water-sensitive drug aspirin is found to form concentrated transparent LTTMs, where it is some 10-fold more stable against cleavage than in water. 2016-07-15T22:11:23Z 2016-07-15T22:11:23Z 2015-08 2015-05 2016-05-23T12:17:44Z Article http://purl.org/eprint/type/JournalArticle 0273-2289 1559-0291 http://hdl.handle.net/1721.1/103634 Su, Erzheng, and Alexander M. Klibanov. “Low-Transition-Temperature Mixtures (LTTMs) for Dissolving Proteins and for Drug Formulation.” Applied Biochemistry and Biotechnology 177, no. 3 (August 4, 2015): 753–758. https://orcid.org/0000-0003-3830-714X en http://dx.doi.org/10.1007/s12010-015-1777-x Applied Biochemistry and Biotechnology Creative Commons Attribution-Noncommercial-Share Alike http://creativecommons.org/licenses/by-nc-sa/4.0/ Springer Science+Business Media New York application/pdf Springer US Springer US
spellingShingle Su, Erzheng
Klibanov, Alexander M.
Low-Transition-Temperature Mixtures (LTTMs) for Dissolving Proteins and for Drug Formulation
title Low-Transition-Temperature Mixtures (LTTMs) for Dissolving Proteins and for Drug Formulation
title_full Low-Transition-Temperature Mixtures (LTTMs) for Dissolving Proteins and for Drug Formulation
title_fullStr Low-Transition-Temperature Mixtures (LTTMs) for Dissolving Proteins and for Drug Formulation
title_full_unstemmed Low-Transition-Temperature Mixtures (LTTMs) for Dissolving Proteins and for Drug Formulation
title_short Low-Transition-Temperature Mixtures (LTTMs) for Dissolving Proteins and for Drug Formulation
title_sort low transition temperature mixtures lttms for dissolving proteins and for drug formulation
url http://hdl.handle.net/1721.1/103634
https://orcid.org/0000-0003-3830-714X
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