Evidence map›Paper›PMID 36768518›Full record

ArticleInternational journal of molecular sciences2023

GxxxG Motif Stabilize Ion-Channel like Pores through C

Carola Rando, Giuseppe Grasso, Dibakar Sarkar, Michele Francesco Maria Sciacca, Lorena Maria Cucci, Alessia Cosentino, Giuseppe Forte, Martina Pannuzzo, Cristina Satriano, Anirban Bhunia and 1 more

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

4 citing papers in PubMed, 9 citations in OpenAlex.

  1. Review
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  4. Review
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

11 authors at 4 institutions in 2 countries.

Carola RandoDipartimento di Scienze Chimiche, Università degli Studi di Catania, Viale A. Doria 6, 95125 Catania, Italy.
Giuseppe GrassoDipartimento di Scienze Chimiche, Università degli Studi di Catania, Viale A. Doria 6, 95125 Catania, Italy.ORCID 0000-0002-7179-4835
Dibakar SarkarDepartment of Biophysics Bose Institute, Unified Academic Campus, Bidhan Nagar, EN 80, Kolkata 700091, India.
Michele Francesco Maria SciaccaConsiglio Nazionale delle Ricerche, Istituto di Cristallografia, 95121 Catania, Italy.ORCID 0000-0002-9981-3321
Lorena Maria CucciDipartimento di Scienze Chimiche, Università degli Studi di Catania, Viale A. Doria 6, 95125 Catania, Italy.ORCID 0000-0001-6127-5962
Alessia CosentinoDipartimento di Scienze Chimiche, Università degli Studi di Catania, Viale A. Doria 6, 95125 Catania, Italy.
Giuseppe ForteDipartimento di Scienze del Farmaco e della Salute, Università degli Studi di Catania, Viale A. Doria 6, 95125 Catania, Italy.ORCID 0000-0002-6607-6038
Martina PannuzzoLaboratory of Nanotechnology for Precision Medicine, Fondazione Istituto Italiano di Tecnologia, Via Morego 30, 16163 Genoa, Italy.
Cristina SatrianoDipartimento di Scienze Chimiche, Università degli Studi di Catania, Viale A. Doria 6, 95125 Catania, Italy.ORCID 0000-0001-5348-5863
Anirban BhuniaDepartment of Biophysics Bose Institute, Unified Academic Campus, Bidhan Nagar, EN 80, Kolkata 700091, India.ORCID 0000-0002-8752-2842
Carmelo La RosaDipartimento di Scienze Chimiche, Università degli Studi di Catania, Viale A. Doria 6, 95125 Catania, Italy.ORCID 0000-0002-7123-5347
University of Catania · ITBose Institute · INInstitute of Crystallography · ITItalian Institute of Technology · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aβ (1-40) can transfer from the aqueous phase to the bilayer and thus form stable ion-channel-like pores where the protein has alpha-helical conformation. The stability of the pores is due to the presence of the GXXXG motif. It has been reported that these ion-channel-like pores are stabilized by a Cα-H···O hydrogen bond that is established between a glycine of the GXXXG sequence of an alpha-helix and another amino acid of a vicinal alpha-helix. However, conflicting data are reported in the literature. Some authors have suggested that hydrogen bonding does not have a stabilizing function. Here we synthesized pentapeptides having a GXXXG motif to explore its role in pore stability. We used molecular dynamics simulations, quantum mechanics, and experimental biophysical techniques to determine whether hydrogen bonding was formed and had a stabilizing function in ion-channel-like structures. Starting from our previous molecular dynamics data, molecular quantum mechanics simulations, and ATR data showed that a stable ion-channel-like pore formed and a band centered at 2910 cm

Indexed as

Amino AcidsIon ChannelsAmyloid beta-PeptidesGlycineHydrogen BondingMolecular ConformationMolecular Dynamics SimulationAmino AcidsAmyloid beta-PeptidesGlycineIon ChannelsAFMAβFTIR-ATRhydrogen bondion-channel-likemembraneporequantum mechanicstoxicity

Identifiers

PMID36768518
PMCPMC9917128
OpenAlexW4317734380

What OpenQuestion holds

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LicenceCC BY
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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.