Evidence map›Paper›PMID 32908463›Full record

ArticleTheScientificWorldJournal2020

Biophysical Insight into the Interaction of Human Lysozyme with Anticancer Drug Anastrozole: A Multitechnique Approach.

Fahad M Almutairi, Mohammad Rehan Ajmal, Adel Ibrahim Al Alawy, Rizwan Hasan Khan, Ali Saber Abdelhameed

Open access · goldAbstract read
In one paragraph

Article in TheScientificWorldJournal, 2020. 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
0.3field-weighted citation impact, top 43% 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, 4 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

5 authors at 3 institutions in 2 countries.

Fahad M AlmutairiPhysical Biochemistry Research Laboratory, Biochemistry Department, Faculty of Science, University of Tabuk, P.O. Box 741, Tabuk 71491, Saudi Arabia.ORCID https://orcid.org/0000-0001-6951-1114
Mohammad Rehan AjmalPhysical Biochemistry Research Laboratory, Biochemistry Department, Faculty of Science, University of Tabuk, P.O. Box 741, Tabuk 71491, Saudi Arabia.ORCID https://orcid.org/0000-0002-2480-9379
Adel Ibrahim Al AlawyPhysical Biochemistry Research Laboratory, Biochemistry Department, Faculty of Science, University of Tabuk, P.O. Box 741, Tabuk 71491, Saudi Arabia.
Rizwan Hasan KhanInterdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, India.ORCID https://orcid.org/0000-0002-9965-8982
Ali Saber AbdelhameedFaculty of Pharmacy, King Saud University, Riyadh, Saudi Arabia.
University of Tabuk · SAAligarh Muslim University · INKing Saud University · SA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the present study, we employ fluorescence spectroscopy, dynamic light scattering, and molecular docking methods. Binding of anticancer drug anastrozole with human lysozyme (HL) is studied. Binding of anastrozole to HL is moderate but spontaneous. There is anastrozole persuaded hydrodynamic change in HL, leading to molecular compaction. Binding of anastrozole to HL also decreased in vitro lytic activity of HL. Molecular docking results suggest the electrostatic interactions and van der Waals forces played key role in binding interaction of anastrozole near the catalytic site. Binding interaction of anastrozole to proteins other than major transport proteins in blood can significantly affect pharmacokinetics of this molecule. Hence, rationalizing drug dosage is important. This study also points to unrelated effects that small molecules bring in the body that are considerable and need thorough investigation.

Indexed as

Molecular Docking SimulationMolecular Dynamics SimulationSpectrum AnalysisAnastrozoleAntineoplastic AgentsEnzyme ActivationHumansMolecular ConformationMolecular StructureMuramidaseProtein BindingStructure-Activity RelationshipAnastrozoleAntineoplastic AgentsMuramidase

Identifiers

PMID32908463
PMCPMC7468670
OpenAlexW3081494005

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.