Evidence map›Paper›PMID 36014578›Full record

ArticleMolecules (Basel, Switzerland)2022

Biophysical Characterization of the Interaction between a Transport Human Plasma Protein and the 5,10,15,20-Tetra(pyridine-4-yl)porphyrin.

Otávio Augusto Chaves, Bernardo A Iglesias, Carlos Serpa

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
2.8field-weighted citation impact, top 8% 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

5 citing papers in PubMed, 34 citations in OpenAlex.

  1. Spectroscopic Analysis of the TiOInternational journal of molecular sciences · 2026
    Article
  2. Article
  3. Article
  4. Porphyrin-Based Compounds: Synthesis and Application.Molecules (Basel, Switzerland) · 2023
    Article
  5. 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

3 authors at 2 institutions in 2 countries.

Otávio Augusto ChavesCQC-IMS, Department of Chemistry, University of Coimbra, Rua Larga, 3004-535 Coimbra, Portugal.ORCID 0000-0001-6211-7659
Bernardo A IglesiasBioinorganic and Porpyrinoids Materials Lab, Department of Chemistry, Federal University of Santa Maria, Santa Maria 97105-900, Brazil.ORCID 0000-0002-4039-6316
Carlos SerpaCQC-IMS, Department of Chemistry, University of Coimbra, Rua Larga, 3004-535 Coimbra, Portugal.
University of Coimbra · PTUniversidade Federal de Santa Maria · BR

Funding

Fundação para a Ciência e Tecnologia UIDB/00313/2020
6 · The paper itself

Abstract

The interaction between human serum albumin (HSA) and the non-charged synthetic photosensitizer 5,10,15,20-tetra(pyridine-4-yl)porphyrin (4-TPyP) was evaluated by in vitro assays under physiological conditions using spectroscopic techniques (UV-vis, circular dichroism, steady-state, time-resolved, synchronous, and 3D-fluorescence) combined with in silico calculations by molecular docking. The UV-vis and steady-state fluorescence parameters indicated a ground-state association between HSA and 4-TPyP and the absence of any dynamic fluorescence quenching was confirmed by the same average fluorescence lifetime for HSA without (4.76 ± 0.11 ns) and with 4-TPyP (4.79 ± 0.14 ns). Therefore, the Stern-Volmer quenching (

Indexed as

PorphyrinsBinding SitesCircular DichroismHumansMolecular Docking SimulationProtein BindingPyridinesSerum AlbuminSerum Albumin, HumanSpectrometry, FluorescenceThermodynamicsPorphyrinsPyridinesSerum AlbuminSerum Albumin, Humanchemical-biological interactionshuman serum albuminmolecular dockingporphyrinspectroscopy

Identifiers

PMID36014578
PMCPMC9413328
OpenAlexW4292973690

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.