Evidence map›Paper›PMID 30121821›Full record

ArticleMolecular biology reports2018

Molecular dynamics simulation as a tool for assessment of drug binding property of human serum albumin.

Meenu Narwal, Deepak Kumar, Tapan Kumar Mukherjee, Rajasri Bhattacharyya, Dibyajyoti Banerjee

Abstract read
PubMed Publisher
In one paragraph

Article in Molecular biology reports, 2018. 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 29% 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, 18 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Albumin as a drug: its biological effects beyond volume expansion.Critical care and resuscitation : journal of the Australasian Academy of Critical Care Medicine · 2020
    Review
  6. 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

5 authors at 2 institutions in 1 country.

Meenu NarwalDepartment of Biotechnology, Maharishi Markandeshwar University, Mullana, Ambala, Haryana, 133203, India.ORCID http://orcid.org/0000-0001-8406-3073
Deepak KumarDepartment of Experimental Medicine and Biotechnology, PGIMER, Chandigarh, 160012, India.ORCID http://orcid.org/0000-0001-6343-6774
Tapan Kumar MukherjeeDepartment of Biotechnology, Maharishi Markandeshwar University, Mullana, Ambala, Haryana, 133203, India.ORCID http://orcid.org/0000-0002-2350-9358
Rajasri BhattacharyyaDepartment of Experimental Medicine and Biotechnology, PGIMER, Chandigarh, 160012, India. bdr.rajasri@yahoo.in.ORCID http://orcid.org/0000-0002-5468-3455
Dibyajyoti BanerjeeDepartment of Experimental Medicine and Biotechnology, PGIMER, Chandigarh, 160012, India. dibyajyoti5200@yahoo.co.in.ORCID http://orcid.org/0000-0003-1690-8139
Post Graduate Institute of Medical Education and Research · INMaharishi Markandeshwar University, Mullana · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human serum albumin (HSA) is a major plasma protein and binding of drugs with this plasma protein has a great importance. It possess esterase activity which can cleave the drugs containing ester bond and thus, can regulate the effect of drugs. Till date no systematic study has been done to analyse binding of such drugs and to compare the results with the drugs which do not have ester bond. Therefore, in the present study two different categories-ester and non-ester drugs have been considered to analyse their interaction with HSA at two principle drug binding sites using molecular modelling tools. It is observed that the drugs irrespective of ester or non-ester nature prefer either Sudlow site I or II by hydrogen bond and hydrophobic interactions. The information obtained from the study can assist to study pharmacokinetics of the drugs and that in turn will help in noval drug discoveries.

Indexed as

Binding SitesEsterasesHumansHydrogen BondingHydrophobic and Hydrophilic InteractionsMolecular Docking SimulationMolecular Dynamics SimulationProtein BindingSerum Albumin, HumanThermodynamicsEsterasesSerum Albumin, HumanDrug–HSA interactionEsterase activityEster drugHSANon-ester drug

Identifiers

PMID30121821
OpenAlexW2885881741

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.