| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 9603113 | Journal of Bioscience and Bioengineering | 2005 | 6 Pages |
Abstract
Protein aggregation is a major obstacle in both biological applications and biomedical fields involving proteins. In this study, we investigated the essential structure of small additives that function as chemical chaperones. Aggregation-suppressing competent additives were 1,3-diaminopropane, 1,4-diaminobutane, and 1,5-diaminopentane, which suppressed aggregation in the given order; whereas no diols or monoamines prevented the thermal aggregation and the inactivation of lysozyme. The heat-inactivation rate of lysozyme with 1,3-diaminopropane was almost identical to that of lysozyme with spermine and arginine ethylester, which are the most prominent additives reported yet.
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Bioengineering
Authors
Masahiro Okanojo, Kentaro Shiraki, Motonori Kudou, Shingo Nishikori, Masahiro Takagi,