Evidence map›Paper›PMID 25456590›Full record

ArticleJournal of chromatography. A2014

Analysis of free drug fractions by ultrafast affinity extraction: interactions of sulfonylurea drugs with normal or glycated human serum albumin.

Xiwei Zheng, Ryan Matsuda, David S Hage

Erratum issuedAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of chromatography. A, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

16 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. 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
  6. 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
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Xiwei ZhengDepartment of Chemistry, University of Nebraska, Lincoln, NE 68588, USA.
Ryan MatsudaDepartment of Chemistry, University of Nebraska, Lincoln, NE 68588, USA.
David S HageDepartment of Chemistry, University of Nebraska, Lincoln, NE 68588, USA. Electronic address: dhage1@unl.edu.
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

Ultrafast affinity extraction and a multi-dimensional affinity system were developed for measuring free drug fractions at therapeutic levels. This approach was used to compare the free fractions and global affinity constants of several sulfonylurea drugs in the presence of normal human serum albumin (HSA) or glycated forms of this protein, as are produced during diabetes. Affinity microcolumns containing immobilized HSA were first used to extract the free drug fractions in injected drug/protein mixtures. As the retained drug eluted from the HSA microcolumn, it was passed through a second HSA column for further separation and measurement. Items that were considered during the optimization of this approach included the column sizes and flow rates that were used, and the time at which the second column was placed on-line with the HSA microcolumn. This method required only 1.0 μL of a sample per injection and was able to measure free drug fractions as small as 0.09-2.58% with an absolute precision of ±0.02-0.5%. The results that were obtained indicated that glycation can affect the free fractions of sulfonylurea drugs at typical therapeutic levels and that the size of this effect varies with the level of HSA glycation. Global affinity constants that were estimated from these free drug fractions gave good agreement with those predicted from previous binding studies or determined through a reference method. The same approach could be utilized with other drugs and proteins or modified binding agents of clinical or pharmaceutical interest.

Indexed as

Chromatography, AffinityGlycated Serum AlbuminGlycation End Products, AdvancedGlycosylationHumansProtein BindingSerum AlbuminSulfonylurea CompoundsTime FactorsGlycated Serum AlbuminGlycation End Products, AdvancedSerum AlbuminSulfonylurea CompoundsAffinity chromatographyDrug–protein bindingHuman serum albuminProtein glycationSulfonylurea drugsUltrafast affinity extraction

Identifiers

PMID25456590
PMCPMC4254497
OpenAlexW1988306054

What OpenQuestion holds

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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.