Evidence map›Paper›PMID 39382238›Full record

ArticleChembiochem : a European journal of chemical biology2024

A Spectroscopic Study on the Amyloid-β Interaction with Clicked Peptide-Porphyrin Conjugates: a Vision Toward the Detection of Aβ Peptides in Aqueous Solution.

Rita Tosto, Stefania Zimbone, Giuseppina Sabatino, Giuseppe Di Natale, Maria Laura Giuffrida, Marianna Flora Tomasello, Luca Lanzanò, Tiziana Campagna, Sonia Covaceuszach, Graziella Vecchio and 1 more

Abstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. KLVFF Functionalized Graphene Oxide for AβSmall (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  2. 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

11 authors.

Rita TostoInstitute of Crystallography, National Research Council, Via Paolo Gaifami 18, 95126, Catania, Italy.
Stefania ZimboneInstitute of Crystallography, National Research Council, Via Paolo Gaifami 18, 95126, Catania, Italy.
Giuseppina SabatinoInstitute of Crystallography, National Research Council, Via Paolo Gaifami 18, 95126, Catania, Italy.
Giuseppe Di NataleInstitute of Crystallography, National Research Council, Via Paolo Gaifami 18, 95126, Catania, Italy.
Maria Laura GiuffridaInstitute of Crystallography, National Research Council, Via Paolo Gaifami 18, 95126, Catania, Italy.
Marianna Flora TomaselloInstitute of Crystallography, National Research Council, Via Paolo Gaifami 18, 95126, Catania, Italy.
Luca LanzanòDepartment of Physics and Astronomy, University of Catania, Viale Andrea Doria, 6, 95125, Catania, Italy.
Tiziana CampagnaInstitute of Crystallography, National Research Council, Via Paolo Gaifami 18, 95126, Catania, Italy.
Sonia CovaceuszachInstitute of Crystallography, National Research Council, Strada Statale 14 Km 16.5, 1434149, Basovizza (TS), Italy.
Graziella VecchioDepartment of Chemical Sciences, University of Catania, Viale Andrea Doria, 6, 95125, Catania, Italy.
Giuseppe PappalardoInstitute of Crystallography, National Research Council, Via Paolo Gaifami 18, 95126, Catania, Italy.ORCID 0000-0001-7328-3492

Funding

Sicilian Micronano-Tech Research and Innovation Center - SAMOTHRACE Ecosistema dell'Innovazione Sicilian Micronano-Tech Research and Innovation Center - SAMOECS00000022 - CUP B63C22000620005.
6 · The paper itself

Abstract

Alzheimer's disease (AD) is a multifactorial form of dementia mainly affecting people in the elderly, but no effective cure is available. According to the amyloid hypothesis the aggregation of Amyloid-β (Aβ) into oligomeric toxic species is believed to concur with the onset and progression of the disease heavily. By using a click chemistry approach, we conjugated a suitable designed peptide sequence to a metalloporphyrin moiety to obtain three hybrid peptide systems to be studied for their interaction with Amyloid-β peptides. The aim is to get new tools for the diagnosis and therapy in AD. The results described in this study, which were obtained through spectroscopic techniques (UV-Vis, CD, bis-Ans and intrinsic porphyrin Fluorescence), Microfluidics (GCI) and cell biology (MTT, Live cell imaging and flow cytometry), reveal interesting features about the structure-activity relationships connecting these conjugates with the interaction with Aβ, as well as on their potential use as sensing systems. In our opinion the data reported in this paper make the porphyrin-peptide conjugates highly compelling for further exploration as spectroscopic probes to detect Aβ biomarkers in biological fluids.

Indexed as

Amyloid beta-PeptidesPorphyrinsAlzheimer DiseaseCircular DichroismClick ChemistryHumansSolutionsSpectrometry, FluorescenceWaterAmyloid beta-PeptidesPorphyrinsSolutionsWaterAlzheimer's Disease (AD)Amyloid sensorAmyloid-β (Aβ)Circular Dichroism (CD)Grating-Coupled Interferometry (GCI)Porphyrins

Identifiers

PMID39382238
PMCPMC11610669

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.