Evidence map›Paper›PMID 24911267›Full record

ArticleAnalytical chemistry2014

Determination of rate constants and equilibrium constants for solution-phase drug-protein interactions by ultrafast affinity extraction.

Xiwei Zheng, Zhao Li, Maria I Podariu, David S Hage

Open access · bronzeAbstract read
In one paragraph

Article in Analytical chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.1field-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

30 citing papers in PubMed, 62 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Analysis of the binding of warfarin to glyoxal- and methylglyoxal-modified human serum albumin by ultrafast affinity extraction.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2022
    Article
  8. Evaluation of microcolumn stability in ultrafast affinity extraction for binding and rate studies.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2021
    Article
  9. Review
  10. Characterization of drug binding with alphaJournal of chromatography. A · 2021
    Article
  11. Article
  12. Affinity chromatography: A review of trends and developments over the past 50 years.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2020
    Review
  13. Article
  14. Article
  15. Article
  16. Kinetic Analysis by Affinity Chromatography.Frontiers in chemistry · 2019
    Review
  17. Article
  18. Article
  19. Mobile Affinity Sorbent Chromatography.Analytical chemistry · 2018
    Article
  20. Review
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

4 authors at 1 institution in 1 country.

Xiwei ZhengDepartment of Chemistry, University of Nebraska , 704 Hamilton Hall, Lincoln, Nebraska 68588, United States.
Zhao Li
Maria I Podariu
David S Hage
University of Nebraska–Lincoln · US

Funding

CHROMATOGRAPHIC AUTOMATION OF IMMUNOASSAYSR01GM044931 · NIGMS · UNIVERSITY OF NEBRASKA LINCOLN · PI HAGE, DAVID S · 1998 to 2014
$2.7M
CHROMATOGRAPHIC STUDIES OF FUNCTIONAL PROTEOMICSR01DK069629 · NIDDK · UNIVERSITY OF NEBRASKA LINCOLN · PI HAGE, DAVID S · 2006 to 2017
$1.8M
NIDDK NIH HHS R01 DK069629NIGMS NIH HHS R01 GM044931
6 · The paper itself

Abstract

A method was created on the basis of ultrafast affinity extraction to determine both the dissociation rate constants and equilibrium constants for drug-protein interactions in solution. Human serum albumin (HSA), an important binding agent for many drugs in blood, was used as both a model soluble protein and as an immobilized binding agent in affinity microcolumns for the analysis of free drug fractions. Several drugs were examined that are known to bind to HSA. Various conditions to optimize in the use of ultrafast affinity extraction for equilibrium and kinetic studies were considered, and several approaches for these measurements were examined. The dissociation rate constants obtained for soluble HSA with each drug gave good agreement with previous rate constants reported for the same drugs or other solutes with comparable affinities for HSA. The equilibrium constants that were determined also showed good agreement with the literature. The results demonstrated that ultrafast affinity extraction could be used as a rapid approach to provide information on both the kinetics and thermodynamics of a drug-protein interaction in solution. This approach could be extended to other systems and should be valuable for high-throughput drug screening or biointeraction studies.

Indexed as

Chromatography, AffinityHumansKineticsPharmaceutical PreparationsProtein BindingSerum AlbuminSolubilityPharmaceutical PreparationsSerum Albumin

Identifiers

PMID24911267
PMCPMC4082384
OpenAlexW2334219519

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.