Methods: We investigated the interaction of CTD-NPM1 regions with model membranes through fluorescence, SPR, CD and ESR spectroscopies and the localization of NPM1 by immune-fluorescence in leukemic cells.

Background: Nucleophosmin-1 (NPM1) is an abundant multifunctional protein, implicated in a variety of biological processes and in the pathogenesis of several human malignancies. Its C-terminal domain (CTD) is endowed with a three helix bundle and we demonstrated that several regions within it, associated with acute myeloid leukemia (AML), have a strong tendency to form beta amyloid-like assemblies toxic for cells. The central helix of the bundle (H2) resulted the most amyloidgenic region; here we aim to model the cytoxicity processes of the H2 sequence and getting clues of a potential involvement in toxicity of the interaction between CTDs and cellular membranes.

Nucleophosmin-1 regions associated with acute myeloid leukemia interact differently with lipid membranes

Di Matteo Adele;
2018

Abstract

Background: Nucleophosmin-1 (NPM1) is an abundant multifunctional protein, implicated in a variety of biological processes and in the pathogenesis of several human malignancies. Its C-terminal domain (CTD) is endowed with a three helix bundle and we demonstrated that several regions within it, associated with acute myeloid leukemia (AML), have a strong tendency to form beta amyloid-like assemblies toxic for cells. The central helix of the bundle (H2) resulted the most amyloidgenic region; here we aim to model the cytoxicity processes of the H2 sequence and getting clues of a potential involvement in toxicity of the interaction between CTDs and cellular membranes.
2018
Istituto di Biologia e Patologia Molecolari - IBPM
Methods: We investigated the interaction of CTD-NPM1 regions with model membranes through fluorescence, SPR, CD and ESR spectroscopies and the localization of NPM1 by immune-fluorescence in leukemic cells.
CD spectroscopy
ESR spectroscopy
Protein-membrane interaction
Nucleophosmin C-terminal domain
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/355497
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