Evidence map›Paper›PMID 27312768›Full record

ArticleScientific reports2016

Organic bioelectronics probing conformational changes in surface confined proteins.

Eleonora Macchia, Domenico Alberga, Kyriaki Manoli, Giuseppe F Mangiatordi, Maria Magliulo, Gerardo Palazzo, Francesco Giordano, Gianluca Lattanzi, Luisa Torsi

Abstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
–field-weighted citation impact
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

11 citing papers in PubMed.

  1. Article
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  6. Review
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  10. A thirst for advancement.Nature materials · 2018
    Article
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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

9 authors.

Eleonora MacchiaDipartimento di Chimica, Università degli Studi di Bari Aldo Moro - Bari (Italy).
Domenico AlbergaDipartimento Interateneo di Fisica "M. Merlin" dell'Università e del Politecnico di Bari - Bari (Italy).
Kyriaki ManoliDipartimento di Chimica, Università degli Studi di Bari Aldo Moro - Bari (Italy).
Giuseppe F MangiatordiDipartimento di Farmacia - Scienze del Farmaco, Università degli Studi di Bari Aldo Moro - Bari (Italy).
Maria MagliuloDipartimento di Chimica, Università degli Studi di Bari Aldo Moro - Bari (Italy).
Gerardo PalazzoDipartimento di Chimica, Università degli Studi di Bari Aldo Moro - Bari (Italy).
Francesco GiordanoDipartimento Interateneo di Fisica "M. Merlin" dell'Università e del Politecnico di Bari - Bari (Italy).
Gianluca LattanziDipartimento di Medicina Clinica e Sperimentale -Università degli Studi di Foggia - Foggia (Italy).
Luisa TorsiDipartimento di Chimica, Università degli Studi di Bari Aldo Moro - Bari (Italy).

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The study of proteins confined on a surface has attracted a great deal of attention due to its relevance in the development of bio-systems for laboratory and clinical settings. In this respect, organic bio-electronic platforms can be used as tools to achieve a deeper understanding of the processes involving protein interfaces. In this work, biotin-binding proteins have been integrated in two different organic thin-film transistor (TFT) configurations to separately address the changes occurring in the protein-ligand complex morphology and dipole moment. This has been achieved by decoupling the output current change upon binding, taken as the transducing signal, into its component figures of merit. In particular, the threshold voltage is related to the protein dipole moment, while the field-effect mobility is associated with conformational changes occurring in the proteins of the layer when ligand binding occurs. Molecular Dynamics simulations on the whole avidin tetramer in presence and absence of ligands were carried out, to evaluate how the tight interactions with the ligand affect the protein dipole moment and the conformation of the loops surrounding the binding pocket. These simulations allow assembling a rather complete picture of the studied interaction processes and support the interpretation of the experimental results.

Indexed as

Biosensing TechniquesBiotinCarrier ProteinsMolecular Dynamics SimulationProtein BindingProtein ConformationSemiconductorsSurface PropertiesBiotinbiotin-binding proteinsCarrier Proteins

Identifiers

PMID27312768
PMCPMC4911579

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Registered trials

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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.