Evidence map›Paper›PMID 34214537›Full record

ArticleBiophysical journal2021

Metallodrug-protein interaction probed by synchrotron terahertz and neutron scattering spectroscopy.

Luis Alberto Esteves Batista de Carvalho, Adriana Pereira Mamede, Ana Lucia Marques Batista de Carvalho, Joana Marques, Gianfelice Cinque, Svemir Rudić, Maria Paula Matos Marques

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

6 citing papers in PubMed, 12 citations in OpenAlex.

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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

7 authors at 3 institutions in 2 countries.

Luis Alberto Esteves Batista de CarvalhoMolecular Physical Chemistry R&D Unit, Department of Chemistry, University of Coimbra, Coimbra, Portugal.
Adriana Pereira MamedeMolecular Physical Chemistry R&D Unit, Department of Chemistry, University of Coimbra, Coimbra, Portugal.
Ana Lucia Marques Batista de CarvalhoMolecular Physical Chemistry R&D Unit, Department of Chemistry, University of Coimbra, Coimbra, Portugal. Electronic address: almbc@uc.pt.
Joana MarquesMolecular Physical Chemistry R&D Unit, Department of Chemistry, University of Coimbra, Coimbra, Portugal.
Gianfelice CinqueDiamond Light Source, Harwell Science and Innovation Campus, Didcot, Oxfordshire, United Kingdom.
Svemir RudićISIS Facility, STFC Rutherford Appleton Laboratory, Didcot, Oxfordshire, United Kingdom.
Maria Paula Matos MarquesMolecular Physical Chemistry R&D Unit, Department of Chemistry, University of Coimbra, Coimbra, Portugal; Department of Life Sciences, University of Coimbra, Coimbra, Portugal.
University of Coimbra · PTDiamond Light Source · GBRutherford Appleton Laboratory · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This experimental work applied coherent synchrotron-radiation terahertz spectroscopy and inelastic neutron scattering to address two processes directly associated with the mode of action of metal-based anticancer agents that can severely undermine chemotherapeutic treatment: drug binding to human serum albumin, occurring during intravenous drug transport, and intracellular coordination to thiol-containing biomolecules (such as metallothioneins) associated with acquired drug resistance. Cisplatin and two dinuclear platinum (Pt)- and palladium (Pd)-polyamine agents developed by this research group, which have yielded promising results toward some types of human cancers, were investigated. Complementary synchrotron-radiation-terahertz and inelastic neutron scattering data revealed protein metalation, through S- and N-donor ligands from cysteine, methionine, and histidine residues. A clear impact of the Pt and Pd agents was evidenced, drug binding to albumin and metallothionein having been responsible for significant changes in the overall protein conformation, as well as for an increased flexibility and possible aggregation.

Indexed as

Antineoplastic AgentsSynchrotronsCisplatinHumansNeutronsSpectrum AnalysisAntineoplastic AgentsCisplatin

Identifiers

PMID34214537
PMCPMC8390959
OpenAlexW3176794606

What OpenQuestion holds

Textmetadata
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.