Evidence map›Paper›PMID 18937061›Full record

ArticleJournal of fluorescence2009

Thermodynamics, conformation and active sites of the binding of Zn-Nd hetero-bimetallic Schiff base to bovine serum albumin.

Qi Xiao, Shan Huang, Yi Liu, Fang-fang Tian, Jun-cheng Zhu

Abstract read
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In one paragraph

Article in Journal of fluorescence, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

9 citing papers in PubMed, 79 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

5 authors at 1 institution in 1 country.

Qi XiaoState Key Laboratory of Virology, College of Chemistry and Molecular Science, Wuhan University, Wuhan, 430072, People's Republic of China.
Shan Huang
Yi Liu
Fang-fang Tian
Jun-cheng Zhu
Wuhan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The interactions between N,N'-di(2-hydroxy-3-methyoxy-phenyl-1-methylene)-o-phenyldiamine-mone Zn(II), Nd(III) nitrate (2LZnNd) and bovine serum albumin (BSA) was investigated by various spectroscopic techniques under physiological conditions. It was proved that the fluorescence quenching of BSA by 2LZnNb was a result of the formation of a non-fluorescent complex with the binding constants of 3.15 x 10(5); 2.72 x 10(5) and 2.44 x 10(5) M(-1) at 298 K, 304 K and 310 K, respectively. A marked increase in the fluorescence anisotropy in the proteinous environments indicates that BSA introduces motional restriction on the drug molecule. The corresponding thermodynamics parameters DeltaH and DeltaS were calculated to be -16.36 kJ mol(-1) and 43.48 J mol(-1) K(-1) via van't Hoff equation. Moreover, the competitive probes experiment revealed that the binding location of 2LZnNb to BSA is in the hydrophobic pocket of site II. The effect of 2LZnNb on the conformation of BSA has been analyzed by means of CD spectrum and three-dimensional fluorescence spectra. The results indicate that the conformation of BSA molecules was changed in the presence of 2LZnNb Schiff base.

Indexed as

ThermodynamicsAnimalsBinding SitesCatalytic DomainNeodymiumOrganometallic CompoundsProtein BindingProtein ConformationSchiff BasesSerum Albumin, BovineZincNeodymiumOrganometallic CompoundsSchiff BasesSerum Albumin, BovineZinc

Identifiers

PMID18937061
OpenAlexW2116326663

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.