Evidence map›Paper›PMID 30250002›Full record

ArticleInternational journal of molecular sciences2018

Artificial Heme Enzymes for the Construction of Gold-Based Biomaterials.

Gerardo Zambrano, Emmanuel Ruggiero, Anna Malafronte, Marco Chino, Ornella Maglio, Vincenzo Pavone, Flavia Nastri, Angela Lombardi

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.3field-weighted citation impact, top 18% 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

7 citing papers in PubMed, 18 citations in OpenAlex.

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  7. Mn-Mimochrome VIFrontiers in chemistry · 2018
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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

8 authors at 3 institutions in 1 country.

Gerardo ZambranoDepartment of Chemical Sciences, University of Napoli "Federico II" Via Cintia, 80126 Napoli, Italy. gerardo.zambrano@unina.it.ORCID 0000-0002-4284-2172
Emmanuel RuggieroDepartment of Chemical Sciences, University of Napoli "Federico II" Via Cintia, 80126 Napoli, Italy. emmanuel.ruggiero@basf.com.
Anna MalafronteDepartment of Chemical Sciences, University of Napoli "Federico II" Via Cintia, 80126 Napoli, Italy. anna.malafronte@unina.it.
Marco ChinoDepartment of Chemical Sciences, University of Napoli "Federico II" Via Cintia, 80126 Napoli, Italy. marco.chino@unina.it.ORCID 0000-0002-0436-3293
Ornella MaglioDepartment of Chemical Sciences, University of Napoli "Federico II" Via Cintia, 80126 Napoli, Italy. ornella.maglio@unina.it.ORCID 0000-0002-7829-1907
Vincenzo PavoneDepartment of Chemical Sciences, University of Napoli "Federico II" Via Cintia, 80126 Napoli, Italy. vincenzo.pavone@unina.it.
Flavia NastriDepartment of Chemical Sciences, University of Napoli "Federico II" Via Cintia, 80126 Napoli, Italy. flavia.nastri@unina.it.
Angela LombardiDepartment of Chemical Sciences, University of Napoli "Federico II" Via Cintia, 80126 Napoli, Italy. alombard@unina.it.ORCID 0000-0002-2013-3009
Istituto Nazionale di Fisica Nucleare, Sezione di Napoli · ITInstitute of Biostructure and Bioimaging · ITUniversity of Naples Federico II · IT

Funding

Ministero dell'Istruzione, dell'Università e della Ricerca PON/MIUR 01_01585
6 · The paper itself

Abstract

Many efforts are continuously devoted to the construction of hybrid biomaterials for specific applications, by immobilizing enzymes on different types of surfaces and/or nanomaterials. In addition, advances in computational, molecular and structural biology have led to a variety of strategies for designing and engineering artificial enzymes with defined catalytic properties. Here, we report the conjugation of an artificial heme enzyme (MIMO) with lipoic acid (LA) as a building block for the development of gold-based biomaterials. We show that the artificial MIMO@LA can be successfully conjugated to gold nanoparticles or immobilized onto gold electrode surfaces, displaying quasi-reversible redox properties and peroxidase activity. The results of this work open interesting perspectives toward the development of new totally-synthetic catalytic biomaterials for application in biotechnology and biomedicine, expanding the range of the biomolecular component aside from traditional native enzymes.

Indexed as

Biocompatible MaterialsCatalysisElectrodesEnzymes, ImmobilizedGoldHemeMetal NanoparticlesOxidation-ReductionThioctic AcidBiocompatible MaterialsEnzymes, ImmobilizedGoldHemeThioctic Acidartificial enzymescatalytic activityfunctional biomaterialsgold nanoparticlesimmobilization strategiesperoxidases

Identifiers

PMID30250002
PMCPMC6213134
OpenAlexW2891779187

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.