Evidence map›Paper›PMID 26797422›Full record

ArticleJournal of chromatography. A2016

Analysis of free drug fractions in serum by ultrafast affinity extraction and two-dimensional affinity chromatography using α1-acid glycoprotein microcolumns.

Cong Bi, Xiwei Zheng, David S Hage

Abstract read
In one paragraph

Article in Journal of chromatography. A, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.2field-weighted citation impact, top 20% 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

11 citing papers in PubMed, 20 citations in OpenAlex.

  1. Review
  2. Article
  3. 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
  4. 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
  5. Review
  6. Characterization of drug binding with alphaJournal of chromatography. A · 2021
    Article
  7. 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
  8. Article
  9. Review
  10. Review
  11. 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

3 authors at 1 institution in 1 country.

Cong BiDepartment of Chemistry, University of Nebraska, Lincoln, NE 68588, USA.
Xiwei ZhengDepartment 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
NIGMS NIH HHS R01 GM044931
6 · The paper itself

Abstract

In the circulatory system, many drugs are reversibly bound to serum proteins such as human serum albumin (HSA) and alpha1-acid glycoprotein (AGP), resulting in both free and protein-bound fractions for these drugs. This report examined the use of microcolumns containing immobilized AGP for the measurement of free drug fractions by ultrafast affinity extraction and a two-dimensional affinity system. Several drugs known to bind AGP were used as models to develop and evaluate this approach. Factors considered during the creation of this method included the retention of the drugs on the microcolumns, the injection flow rate, the microcolumn size, and the times at which a second AGP column was placed on-line with the microcolumn. The final system had residence times of only 110-830ms during sample passage through the AGP microcolumns and allowed free drug fractions to be determined within 10-20min when using only 3-10μL of sample per injection. This method was used to measure the free fractions of the model drugs at typical therapeutic levels in serum, giving good agreement with the results obtained by ultrafiltration. This approach was also used to estimate the binding constants for each drug with AGP in serum, even for drugs that had significant interactions with both AGP and HSA in such samples. These results indicated that AGP microcolumns could be used with ultrafast affinity extraction to measure free drug fractions in a label-free manner and to study the binding of drugs with AGP in complex samples such as serum.

Indexed as

Chromatography, AffinityHumansImmobilized ProteinsOrosomucoidPharmaceutical PreparationsProtein BindingSerum AlbuminStereoisomerismImmobilized ProteinsOrosomucoidPharmaceutical PreparationsSerum AlbuminDrug-protein bindingFree drug fractionHuman serum albuminUltrafast affinity extractionα(1)-Acid glycoprotein

Identifiers

PMID26797422
PMCPMC4724389
OpenAlexW2206109313

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.