Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

Spermine Oxidase-Substrate Electrostatic Interactions: The Modulation of Enzyme Function by Neighboring Colloidal Ɣ-Fe2O3

Graziano Rilievo
,
Massimiliano Magro
,
Federica Tonolo
ORCID logo ,
Alessandro Cecconello
,
Lavinia Rutigliano
ORCID logo ,
Aura Cencini
,
Simone Molinari
ORCID logo ,
Maria Luisa Di Paolo
ORCID logo ,
Cristian Fiorucci
ORCID logo ,
Marianna Nicoletta Rossi
ORCID logo ,
Manuela Cervelli
* ORCID logo ,
Fabio Vianello
ORCID logo
Version 1 : Received: 8 November 2023 / Approved: 9 November 2023 / Online: 9 November 2023 (07:46:27 CET)

A peer-reviewed article of this Preprint also exists.

Rilievo, G.; Magro, M.; Tonolo, F.; Cecconello, A.; Rutigliano, L.; Cencini, A.; Molinari, S.; Di Paolo, M.L.; Fiorucci, C.; Rossi, M.N.; Cervelli, M.; Vianello, F. Spermine Oxidase–Substrate Electrostatic Interactions: The Modulation of Enzyme Function by Neighboring Colloidal ɣ-Fe2O3. Biomolecules 2023, 13, 1800. Rilievo, G.; Magro, M.; Tonolo, F.; Cecconello, A.; Rutigliano, L.; Cencini, A.; Molinari, S.; Di Paolo, M.L.; Fiorucci, C.; Rossi, M.N.; Cervelli, M.; Vianello, F. Spermine Oxidase–Substrate Electrostatic Interactions: The Modulation of Enzyme Function by Neighboring Colloidal ɣ-Fe2O3. Biomolecules 2023, 13, 1800.

Abstract

Protein–nanoparticle hybridization can ideally lead to novel biological entities characterized by emerging properties, which can sensibly differ from those of the parent components. Herein, the effect of ionic strength on the biological functions of recombinant, His-tagged spermine oxidase (i.e., SMOX) was studied for the first time. Moreover, SMOX was integrated to colloidal surface active maghemite nanoparticles (SAMNs) by direct self-assembly, leading to a biologically active nano-enzyme (i.e., SAMN@SMOX). The hybrid was subjected to an in-depth chemical-physical characterization highlighting that protein structure was perfectly preserved. The catalytic activity of the nanostructured hybrid (SAMN@SMOX) was assessed by extracting kinetics parameters using spermine as substrate and compared to the soluble enzyme as a function of ionic strength. Results revealed that the catalytic function was dominated by electrostatic interactions and that they were drastically modified upon hybridization with colloidal ɣ-Fe2O3. Noteworthy, the affinity of SMOX toward spermine was significantly higher for the nanohybrid at low salinity. The present study supports the vision of using protein–nanoparticle conjugation as a mean for modulating biological functions.

Keywords

Nanoenzyme; Spermine oxidase; Enzyme activity; Electrostatic interactions; Ionic strength; Enzyme nano-immobilization

Subject

Biology and Life Sciences, Biochemistry and Molecular Biology

Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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