title: Diamines prevent thermal aggregation and inactivation of lysozyme.
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.
authors.affiliation: School of Materials Science, Japan Advanced Institute of Science and Technology, 1-1 Asahidai, Nomi, Ishikawa 923-1292, Japan.
authors.forename: Masahiro
authors.initials: M
authors.lastname: Okanojo
authors.forename: Kentaro
authors.initials: K
authors.lastname: Shiraki
authors.forename: Motonori
authors.initials: M
authors.lastname: Kudou
authors.forename: Shingo
authors.initials: S
authors.lastname: Nishikori
authors.forename: Masahiro
authors.initials: M
authors.lastname: Takagi
mesh_terms: D000588:Amines / Q000737:chemistry*; D000818:Animals; D002645:Chickens; D004789:Enzyme Activation; D018832:Molecular Chaperones / Q000737:chemistry*; D009113:Muramidase / Q000737:chemistry*; D017510:Protein Folding
chemical_list: D000588:Amines; D018832:Molecular Chaperones; D009113:Muramidase