Evidence map›Paper›PMID 24349966›Full record

ArticleCurrent Metabolomics2013

Effects of Fatty Acids and Glycation on Drug Interactions with Human Serum Albumin.

Jeanethe A Anguizola, Sara B G Basiaga, David S Hage

Open access · greenAbstract read
In one paragraph

Article in Current Metabolomics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

17 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
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  11. Chromatographic analysis of the effects of fatty acids and glycation on binding by probes for Sudlow sites I and II to human serum albumin.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2016
    Article
  12. Article
  13. Review
  14. Article
  15. Studies of metabolite-protein interactions: a review.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2014
    Review
  16. Article
  17. 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

3 authors at 1 institution in 1 country.

Jeanethe A AnguizolaChemistry Department, University of Nebraska-Lincoln, 704 Hamilton Hall, Lincoln, NE 68588-0304, USA.
Sara B G BasiagaChemistry Department, University of Nebraska-Lincoln, 704 Hamilton Hall, Lincoln, NE 68588-0304, USA.
David S HageChemistry Department, University of Nebraska-Lincoln, 704 Hamilton Hall, Lincoln, NE 68588-0304, USA.
University of Nebraska–Lincoln · US

Funding

EXTRAMURAL RESEARCH FACILITIES CONSTRUCTIONC06RR015468 · NCRR · UNIVERSITY OF NEBRASKA LINCOLN · PI PAUL, PREM S · 2000 to 2000
$2.0M
CHROMATOGRAPHIC STUDIES OF FUNCTIONAL PROTEOMICSR01DK069629 · NIDDK · UNIVERSITY OF NEBRASKA LINCOLN · PI HAGE, DAVID S · 2006 to 2017
$1.8M
NCRR NIH HHS C06 RR015468NIDDK NIH HHS R01 DK069629
6 · The paper itself

Abstract

The presence of elevated glucose concentrations in diabetes is a metabolic change that leads to an increase in the amount of non-enzymatic glycation that occurs for serum proteins. One protein that is affected by this process is the main serum protein, human serum albumin (HSA), which is also an important carrier agent for many drugs and fatty acids in the circulatory system. Sulfonylureas drugs, used to treat type 2 diabetes, are known to have significant binding to HSA. This study employed ultrafiltration and high-performance affinity chromatography to examine the effects of HSA glycation on the interactions of several sulfonylurea drugs (i.e., acetohexamide, tolbutamide and gliclazide) with fatty acids, whose concentrations in serum are also affected by diabetes. Similar overall changes in binding were noted for these drugs with normal HSA or glycated HSA and in the presence of the fatty acids. For most of the tested drugs, the addition of physiological levels of the fatty acids to normal HSA and glycated HSA produced weaker binding. At low fatty acid concentrations, many of these systems followed a direct competition model while others involved a mixed-mode interaction. In some cases, there was a change in the interaction mechanism between normal HSA and glycated HSA, as seen with linoleic acid. Systems with only direct competition also gave notable changes in the affinities of fatty acids at their sites of drug competition when comparing normal HSA and glycated HSA. This research demonstrated the importance of considering how changes in the concentrations and types of metabolites (e.g., in this case, glucose and fatty acids) can alter the function of a protein such as HSA and its ability to interact with drugs or other agents.

Indexed as

Diabetesdrug-protein bindingfatty acidsglycationhigh-performance affinity chromatographyhuman serum albuminsulfonylurea drugsultrafiltration

Identifiers

PMID24349966
PMCPMC3860187
OpenAlexW2008424444

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.