Generic placeholder image

Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Structural Changes and Aggregation Process of Cu/Containing Amine Oxidase in the Presence of 2,2,2-Trifluoroethanol

Author(s): M. Amani, R. Yousefi, A. A. Moosavi-Movahedi, F. Pintus, A. Mura, G. Floris, B. I. Kurganov and A. A. Saboury

Volume 15, Issue 5, 2008

Page: [521 - 527] Pages: 7

DOI: 10.2174/092986608784567636

Price: $65

Abstract

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 β-sheet to α-helix and up to 10% TFE a structural transition from α-helix to β-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 α-helix content. The obtained results revealed that the aggregation of LSAO is strongly linked to the nature of secondary structures.

Keywords: Amine oxidase, TFE, Secondary structure, Circular dichroism, Fluorescence, Aggregation


Rights & Permissions Print Cite
© 2024 Bentham Science Publishers | Privacy Policy