Evidence map›Paper›PMID 38014394›Full record

ArticleCrystEngComm2023

Computation meets experiment: identification of highly efficient fibrillating peptides.

Lorenzo Sori, Andrea Pizzi, Greta Bergamaschi, Alessandro Gori, Alfonso Gautieri, Nicola Demitri, Monica Soncini, Pierangelo Metrangolo

Open access · hybridAbstract read
In one paragraph

Article in CrystEngComm, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 74% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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.

Lorenzo SoriLaboratory of Supramolecular and BioNano Materials (SupraBioNanoLab), Department of Chemistry, Materials, and Chemical Engineering "Giulio Natta", Politecnico di Milano Via Luigi Mancinelli 7 20131 Milan Italy andrea.pizzi@polimi.it pierangelo.metrangolo@polimi.it.ORCID https://orcid.org/0000-0003-4002-638X
Andrea PizziLaboratory of Supramolecular and BioNano Materials (SupraBioNanoLab), Department of Chemistry, Materials, and Chemical Engineering "Giulio Natta", Politecnico di Milano Via Luigi Mancinelli 7 20131 Milan Italy andrea.pizzi@polimi.it pierangelo.metrangolo@polimi.it.ORCID https://orcid.org/0000-0002-4180-9151
Greta BergamaschiIstituto di Scienze e Tecnologie Chimiche - National Research Council of Italy (SCITEC-CNR) 20131 Milan Italy.ORCID https://orcid.org/0000-0002-4501-4057
Alessandro GoriIstituto di Scienze e Tecnologie Chimiche - National Research Council of Italy (SCITEC-CNR) 20131 Milan Italy.
Alfonso GautieriDepartment of Electronics, Information and Bioengineering, Politecnico di Milano 20131 Milan Italy.ORCID https://orcid.org/0000-0003-0492-0130
Nicola DemitriElettra - Sincrotrone Trieste S.S. 14 Km 163.5 in Area Science Park 34149 Basovizza - Trieste Italy.ORCID https://orcid.org/0000-0003-0288-3233
Monica SonciniDepartment of Electronics, Information and Bioengineering, Politecnico di Milano 20131 Milan Italy.ORCID https://orcid.org/0000-0001-8607-7196
Pierangelo MetrangoloLaboratory of Supramolecular and BioNano Materials (SupraBioNanoLab), Department of Chemistry, Materials, and Chemical Engineering "Giulio Natta", Politecnico di Milano Via Luigi Mancinelli 7 20131 Milan Italy andrea.pizzi@polimi.it pierangelo.metrangolo@polimi.it.ORCID https://orcid.org/0000-0002-7945-099X
Politecnico di Milano · ITNational Research Council · ITElettra-Sincrotrone Trieste S.C.p.A. · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Self-assembling peptides are of huge interest for biological, medical and nanotechnological applications. The enormous chemical variety that is available from the 20 amino acids offers potentially unlimited peptide sequences, but it is currently an issue to predict their supramolecular behavior in a reliable and cheap way. Herein we report a computational method to screen and forecast the aqueous self-assembly propensity of amyloidogenic pentapeptides. This method was found also as an interesting tool to predict peptide crystallinity, which may be of interest for the development of peptide based drugs.

Identifiers

PMID38014394
PMCPMC10424810
OpenAlexW4383041471

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.