Evidence map›Paper›PMID 26381571›Full record

ArticleJournal of chromatography. A2015

Analysis of drug-protein binding using on-line immunoextraction and high-performance affinity microcolumns: Studies with normal and glycated human serum albumin.

Ryan Matsuda, Donald Jobe, Jared Beyersdorf, David S Hage

Abstract read
In one paragraph

Article in Journal of chromatography. A, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

15 citing papers in PubMed, 21 citations in OpenAlex.

  1. Characterization of binding by sulfonylureas with normal or modified human serum albumin using affinity microcolumns prepared by entrapment.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2023
    Article
  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. Characterization of drug binding with alphaJournal of chromatography. A · 2021
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Chromatographic studies of chlorpropamide interactions with normal and glycated human serum albumin based on affinity microcolumns.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2018
    Article
  13. Review
  14. Review
  15. Studies of drug interactions with alphaJournal of chromatography. A · 2017
    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

4 authors at 1 institution in 1 country.

Ryan MatsudaDepartment of Chemistry, University of Nebraska-Lincoln, Lincoln, NE 68588-0304, USA.
Donald JobeDepartment of Chemistry, University of Nebraska-Lincoln, Lincoln, NE 68588-0304, USA.
Jared BeyersdorfDepartment of Chemistry, University of Nebraska-Lincoln, Lincoln, NE 68588-0304, USA.
David S HageDepartment of Chemistry, University of Nebraska-Lincoln, Lincoln, NE 68588-0304, 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

A method combining on-line immunoextraction microcolumns with high-performance affinity chromatography (HPAC) was developed and tested for use in examining drug-protein interactions with normal or modified proteins. Normal human serum albumin (HSA) and glycated HSA were used as model proteins for this work. High-performance immunoextraction microcolumns with sizes of 1.0-2.0 cm × 2.1mm i.d. and containing anti-HSA polyclonal antibodies were developed and tested for their ability to bind normal HSA or glycated HSA. These microcolumns were able to extract up to 82-93% for either type of protein at 0.05-0.10 mL/min and had a binding capacity of 0.34-0.42 nmol HSA for a 1.0 cm × 2.1mm i.d. microcolumn. The immunoextraction microcolumns and their adsorbed proteins were tested for use in various approaches for drug binding studies. Frontal analysis was used with the adsorbed HSA/glycated HSA to measure the overall affinities of these proteins for the drugs warfarin and gliclazide, giving comparable values to those obtained previously using similar protein preparations that had been covalently immobilized within HPAC columns. Zonal elution competition studies with gliclazide were next performed to examine the specific interactions of this drug at Sudlow sites I and II of the adsorbed proteins. These results were also comparable to those noted in prior work with covalently immobilized samples of normal HSA or glycated HSA. These experiments indicated that drug-protein binding studies can be carried out by using on-line immunoextraction microcolumns with HPAC. The same method could be used in the future with clinical samples and other drugs or proteins of interest in pharmaceutical studies or biomedical research.

Indexed as

Drug InteractionsAnticoagulantsChromatography, AffinityGliclazideGlycosylationHumansHypoglycemic AgentsProtein BindingSerum AlbuminWarfarinAnticoagulantsGliclazideHypoglycemic AgentsSerum AlbuminWarfarinAffinity microcolumnDrug–protein bindingGlycationHigh-performance affinity chromatographyHuman serum albuminImmunoextraction

Identifiers

PMID26381571
PMCPMC4587353
OpenAlexW1415764313

What OpenQuestion holds

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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.