Evidence map›Paper›PMID 36293026›Full record

ArticleInternational journal of molecular sciences2022

Acidic Shift of Optimum pH of Bovine Serum Amine Oxidase upon Immobilization onto Nanostructured Ferric Tannates.

Graziano Rilievo, Alessandro Cecconello, Simone Molinari, Andrea Venerando, Lavinia Rutigliano, Gayathri T Govardhan, Dinusha H Kariyawasam, Ruth J Arusei, Lucio Zennaro, Maria L Di Paolo and 3 more

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.6field-weighted citation impact, top 35% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors at 2 institutions in 1 country.

Graziano RilievoDepartment of Comparative Biomedicine and Food Science, University of Padua, Viale dell'Università 16, 35020 Legnaro, Italy.
Alessandro CecconelloDepartment of Comparative Biomedicine and Food Science, University of Padua, Viale dell'Università 16, 35020 Legnaro, Italy.
Simone MolinariDepartment of Geosciences, University of Padua, Via Gradenigo 6, 35131 Padova, Italy.ORCID 0000-0003-4105-4833
Andrea VenerandoDepartment of Comparative Biomedicine and Food Science, University of Padua, Viale dell'Università 16, 35020 Legnaro, Italy.
Lavinia RutiglianoDepartment of Molecular Medicine, Sapienza University of Rome, Viale Regina Elena 291, 00161 Rome, Italy.
Gayathri T GovardhanDepartment of Comparative Biomedicine and Food Science, University of Padua, Viale dell'Università 16, 35020 Legnaro, Italy.
Dinusha H KariyawasamDepartment of Comparative Biomedicine and Food Science, University of Padua, Viale dell'Università 16, 35020 Legnaro, Italy.
Ruth J AruseiDepartment of Comparative Biomedicine and Food Science, University of Padua, Viale dell'Università 16, 35020 Legnaro, Italy.
Lucio ZennaroDepartment of Molecular Medicine, University of Padua, via Gabelli 63, 35121 Padova, Italy.
Maria L Di PaoloDepartment of Molecular Medicine, University of Padua, via Gabelli 63, 35121 Padova, Italy.ORCID 0000-0002-2370-9333
Enzo AgostinelliDepartment of Sensory Organs, Sapienza University of Rome, Policlinico Umberto I, Viale del Policlinico 155, 00161 Rome, Italy.ORCID 0000-0002-2508-8868
Fabio VianelloDepartment of Comparative Biomedicine and Food Science, University of Padua, Viale dell'Università 16, 35020 Legnaro, Italy.ORCID 0000-0002-4874-7205
Massimiliano MagroDepartment of Comparative Biomedicine and Food Science, University of Padua, Viale dell'Università 16, 35020 Legnaro, Italy.
University of Padua · ITPoliclinico Umberto I · IT

Funding

Department of Comparative Biomedicine and Food Science, University of Padova "Giovani Ricercatori-Third call"Italian Ministry of Education, University and Research REACT EU - PON "Ricerca e Innovazione 2014-2020"
6 · The paper itself

Abstract

Protein-nanoparticle hybrids represent entities characterized by emerging biological properties that can significantly differ from those of the parent components. Herein, bovine serum amine oxidase (i.e., BSAO) was immobilized onto a magnetic nanomaterial constituted of surface active maghemite nanoparticles (i.e., SAMNs, the core), surface-modified with tannic acid (i.e., TA, the shell), to produce a biologically active ternary hybrid (i.e., SAMN@TA@BSAO). In comparison with the native enzyme, the secondary structure of the immobilized BSAO responded to pH variations sensitively, resulting in a shift of its optimum activity from pH 7.2 to 5.0. Conversely, the native enzyme structure was not influenced by pH and its activity was affected at pH 5.0, i.e., in correspondence with the best performances of SAMN@TA@BSAO. Thus, an extensive NMR study was dedicated to the structure-function relationship of native BSAO, confirming that its low activity below pH 6.0 was ascribable to minimal structural modifications not detected by circular dichroism. The generation of cytotoxic products, such as aldehydes and H

Indexed as

Amine Oxidase (Copper-Containing)NanostructuresAldehydesHydrogen-Ion ConcentrationHydrogen PeroxideIronOxidoreductasesPolyaminesTanninsAldehydesAmine Oxidase (Copper-Containing)Hydrogen PeroxideIronOxidoreductasesPolyaminesTanninsbovine serum amine oxidaseenzyme activityenzyme–nanoparticle hybridsNMR relaxometrypH dependencepolyaminesprotein nano-immobilization

Identifiers

PMID36293026
PMCPMC9603626
OpenAlexW4304806800

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.