Evidence map›Paper›PMID 36768492›Full record

ArticleInternational journal of molecular sciences2023

Enantioselective Human Serum Albumin Binding of Apremilast: Liquid Chromatographic, Fluorescence and Molecular Docking Study.

Gergely Dombi, Péter Horváth, Béla Fiser, Arash Mirzahosseini, Máté Dobó, Zoltán-István Szabó, Gergő Tóth

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Impact of Sinapic Acid on Bovine Serum Albumin Thermal Stability.International journal of molecular sciences · 2024
    Article
  7. Article
  8. 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

7 authors.

Gergely DombiDepartment of Pharmaceutical Chemistry, Semmelweis University, H-1085 Budapest, Hungary.
Péter HorváthDepartment of Pharmaceutical Chemistry, Semmelweis University, H-1085 Budapest, Hungary.ORCID 0000-0001-7149-4173
Béla FiserHigher Education and Industrial Cooperation Centre, University of Miskolc, Egyetemváros, H-3515 Miskolc, Hungary.ORCID 0000-0003-0603-4626
Arash MirzahosseiniDepartment of Pharmaceutical Chemistry, Semmelweis University, H-1085 Budapest, Hungary.ORCID 0000-0002-3281-8435
Máté DobóDepartment of Pharmaceutical Chemistry, Semmelweis University, H-1085 Budapest, Hungary.
Zoltán-István SzabóDepartment of Pharmaceutical Industry and Management, Faculty of Pharmacy, George Emil Palade University of Medicine, Pharmacy, Science, and Technology of Targu Mures, 540142 Targu Mures, Romania.ORCID 0000-0002-8740-0212
Gergő TóthDepartment of Pharmaceutical Chemistry, Semmelweis University, H-1085 Budapest, Hungary.ORCID 0000-0001-5341-319X

Funding

Hungarian Academy of Sciences Bolyai János Kutatói ÖsztöndíjMinistry for Innovation and Technology Bolyai + New National Excellence ProgramNational Research, Development, and Innovation Fund TKP2021-NVA-14Semmelweis University EFOP-3.6.3-VEKOP-16-2017-00009
6 · The paper itself

Abstract

The interaction between human serum albumin (HSA) and apremilast (APR), a novel antipsoriatic drug, was characterized by multimodal analytical techniques including high-performance liquid chromatography (HPLC), fluorescence spectroscopy and molecular docking for the first time. Using an HSA chiral stationary phase, the APR enantiomers were well separated, indicating enantioselective binding between the protein and the analytes. The influence of chromatographic parameters-type and concentration of the organic modifier, buffer type, pH, ionic strength of the mobile phase, flow rate and column temperature-on the chromatographic responses (retention factor and selectivity) was analyzed in detail. The results revealed that the eutomer

Indexed as

Serum AlbuminSerum Albumin, HumanBinding SitesChromatography, High Pressure LiquidHumansMolecular Docking SimulationProtein BindingSpectrometry, FluorescenceStereoisomerismThalidomideThermodynamicsapremilastSerum AlbuminSerum Albumin, HumanThalidomideapremilastchiral chromatographydrug deliveryHSA binding

Identifiers

PMID36768492
PMCPMC9916978

What Socratic 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 Socratic graph.