Evidence map›Paper›PMID 35682687›Full record

ArticleInternational journal of molecular sciences2022

Influence of Cortisol on the Fibril Formation Kinetics of Aβ42 Peptide: A Multi-Technical Approach.

Alessandro Nucara, Francesca Ripanti, Simona Sennato, Giacomo Nisini, Emiliano De Santis, Mahta Sefat, Marina Carbonaro, Dalila Mango, Velia Minicozzi, Marilena Carbone

Open access · goldAbstract read
PubMed Full text at PMC Publisher
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
0.2field-weighted citation impact, top 48% 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, 2 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

10 authors at 5 institutions in 2 countries.

Alessandro NucaraDepartment of Physics, Sapienza University of Rome, P. le A. Moro 5, 00185 Rome, Italy.ORCID 0000-0002-7088-4820
Francesca RipantiDepartment of Physics and Geology, University of Perugia, Via Alessandro Pascoli, 06123 Perugia, Italy.ORCID 0000-0002-9505-740X
Simona SennatoCNR-ISC Sede Sapienza, Department of Physics, Sapienza University, P.le A. Moro 5, 00185 Rome, Italy.ORCID 0000-0003-4793-5359
Giacomo NisiniDepartment of Physics, Sapienza University of Rome, P. le A. Moro 5, 00185 Rome, Italy.ORCID 0000-0003-4555-2469
Emiliano De SantisDepartment of Physics and Astronomy and Department of Chemistry-BMC, Uppsala University, Husargatan 3, 752 37 Uppsala, Sweden.ORCID 0000-0001-5029-7429
Mahta SefatSchool of Pharmacy, Tor Vergata University of Rome, Via della Ricerca Scientifica 1, 00133 Rome, Italy.
Marina CarbonaroCouncil for Agricultural Research and Economics (CREA), Research Centre for Food and Nutrition, Via Ardeatina 546, 00178 Rome, Italy.
Dalila MangoSchool of Pharmacy, Tor Vergata University of Rome, Via della Ricerca Scientifica 1, 00133 Rome, Italy.
Velia MinicozziDepartment of Physics and INFN, Tor Vergata University of Rome, Via della Ricerca Scientifica 1, 00133 Rome, Italy.ORCID 0000-0001-9851-9932
Marilena CarboneDepartment of Chemical Science and Technologies, University of Rome Tor Vergata, Via della Ricerca Scientifica 1, 00133 Rome, Italy.ORCID 0000-0002-4224-1393
University of Rome Tor Vergata · ITSapienza University of Rome · ITConsiglio per la ricerca in agricoltura e l’analisi dell’economia agraria · ITUniversity of Perugia · ITUppsala University · SE

Funding

Sapienza University of Rome progetti di ricerca
6 · The paper itself

Abstract

Amyloid-β peptide (Aβ) aggregates are known to be correlated with pathological neurodegenerative diseases. The fibril formation process of such peptides in solution is influenced by several factors, such as the ionic strength of the buffer, concentration, pH, and presence of other molecules, just to mention a few. In this paper, we report a detailed analysis of in vitro Aβ42 fibril formation in the presence of cortisol at different relative concentrations. The thioflavin T fluorescence assay allowed us to monitor the fibril formation kinetics, while a morphological characterization of the aggregates was obtained by atomic force microscopy. Moreover, infrared absorption spectroscopy was exploited to investigate the secondary structure changes along the fibril formation path. Molecular dynamics calculations allowed us to understand the intermolecular interactions with cortisol. The combined results demonstrated the influence of cortisol on the fibril formation process: indeed, at cortisol-Aβ42 concentration ratio (ρ) close to 0.1 a faster organization of Aβ42 fragments into fibrils is promoted, while for ρ = 1 the formation of fibrils is completely inhibited.

Indexed as

Amyloid beta-PeptidesHydrocortisoneAmyloidKineticsPeptide FragmentsAmyloidAmyloid beta-Peptidesamyloid beta-protein (1-42)HydrocortisonePeptide Fragmentsatomic force microscopyAβ42 peptidefibril formationinfrared spectroscopymolecular dynamicssecondary structureThT fluorescence

Identifiers

PMID35682687
PMCPMC9180743
OpenAlexW4281781365

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.