Evidence map›Paper›PMID 26189669›Full record

ArticleJournal of chromatography. A2015

Analysis of multi-site drug-protein interactions by high-performance affinity chromatography: Binding by glimepiride to normal or glycated human serum albumin.

Ryan Matsuda, Zhao Li, Xiwei Zheng, David S Hage

Erratum issuedOpen access · greenAbstract read
PubMed Full text at PMC Publisher
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. 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
2.4field-weighted citation impact, top 11% 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, 36 citations in OpenAlex.

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  9. 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
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4 · The record

Corrections and comments

  • Erratum issued
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.
Zhao LiDepartment of Chemistry, University of Nebraska-Lincoln, Lincoln, NE 68588-0304, USA.
Xiwei ZhengDepartment 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 STUDIES OF FUNCTIONAL PROTEOMICSR01DK069629 · NIDDK · UNIVERSITY OF NEBRASKA LINCOLN · PI HAGE, DAVID S · 2006 to 2017
$1.8M
NIDDK NIH HHS R01 DK069629
6 · The paper itself

Abstract

High-performance affinity chromatography (HPAC) was used in a variety of formats to examine multi-site interactions between glimepiride, a third-generation sulfonylurea drug, and normal or in vitro glycated forms of the transport protein human serum albumin (HSA). Frontal analysis revealed that glimepiride interacts with normal HSA and glycated HSA at a group of high affinity sites (association equilibrium constant, or Ka, 9.2-11.8×10(5)M(-1) at pH 7.4 and 37°C) and a group of lower affinity regions (Ka, 5.9-16×10(3)M(-1)). Zonal elution competition studies were designed and carried out in both normal- and reversed-role formats to investigate the binding by this drug at specific sites. These experiments indicated that glimepiride was interacting at both Sudlow sites I and II. Allosteric effects were also noted with R-warfarin at Sudlow site I and with tamoxifen at the tamoxifen site on HSA. The binding at Sudlow site I had a 2.1- to 2.3-fold increase in affinity in going from normal HSA to the glycated samples of HSA. There was no significant change in the affinity for glimepiride at Sudlow site II in going from normal HSA to a moderately glycated sample of HSA, but a slight decrease in affinity was seen in going to a more highly glycated HSA sample. These results demonstrated how various HPAC-based methods can be used to profile and characterize multi-site binding by a drug such as glimepiride to a protein and its modified forms. The information obtained from this study should be useful in providing a better understanding of how drug-protein binding may be affected by glycation and of how separation and analysis methods based on HPAC can be employed to study systems with complex interactions or that involve modified proteins.

Indexed as

Binding SitesChromatography, AffinityDigitoxinGlycated Serum AlbuminGlycation End Products, AdvancedGlycosylationHumansProtein BindingSerum AlbuminSulfonylurea CompoundsTamoxifenWarfarinDigitoxinglimepirideGlycated Serum AlbuminGlycation End Products, AdvancedSerum AlbuminSulfonylurea CompoundsTamoxifenWarfarinDrug–protein bindingGlimepirideGlycationHigh-performance affinity chromatographyHuman serum albumin

Identifiers

PMID26189669
PMCPMC4574489
OpenAlexW856909439

What OpenQuestion holds

Textmetadata
LicenceTDM
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.