Structural changes and aggregation process of Cu/containing amine oxidase in the presence of 2,2,2'-trifluoroethanol.
Conformational and structural changes of lentil seedlings amine oxidase (LSAO) were studied in the presence of trifluoroethanol (TFE) by spectroscopic and analytical techniques. At TFE concentrations up to 5%, the induction of a structural transition from beta-sheet to alpha-helix and up to 10% TFE a structural transition from alpha-helix to beta-sheet as well as inactivation of the enzyme are observed. At TFE concentrations between 10-35%, LSAO proves to be prone to aggregation and beyond 35% TFE leads to a non-native protein structure with a high alpha-helix content. The obtained results revealed that the aggregation of LSAO is strongly linked to the nature of secondary structures.
Amani
M
M
Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran.
Yousefi
R
R
Moosavi-Movahedi
A A
AA
Pintus
F
F
Mura
A
A
Floris
G
G
Kurganov
B I
BI
Saboury
A A
AA
D006631:Amine Oxidase (Copper-Containing) / Q000737:chemistry* / Q000302:isolation & purification; D002942:Circular Dichroism; D006358:Hot Temperature; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D014270:Trifluoroethanol / Q000494:pharmacology*
D014270:Trifluoroethanol; D006631:Amine Oxidase (Copper-Containing)