Evidence map›Paper›PMID 29403802›Full record

ArticleJournal of pharmaceutical analysis2013

Reversed-phase fused-core HPLC modeling of peptides.

Matthias D'Hondt, Bert Gevaert, Sofie Stalmans, Sylvia Van Dorpe, Evelien Wynendaele, Kathelijne Peremans, Christian Burvenich, Bart De Spiegeleer

Abstract read
In one paragraph

Article in Journal of pharmaceutical analysis, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
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

6 citing papers in PubMed.

  1. Two Antimicrobial Peptides Derived fromMolecules (Basel, Switzerland) · 2023
    Article
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  3. Article
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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

8 authors.

Matthias D'HondtDrug Quality and Registration (DruQuaR) group, Faculty of Pharmaceutical Sciences, Ghent University, Harelbekestraat 72, B-9000 Ghent, Belgium.
Bert GevaertDrug Quality and Registration (DruQuaR) group, Faculty of Pharmaceutical Sciences, Ghent University, Harelbekestraat 72, B-9000 Ghent, Belgium.
Sofie StalmansDrug Quality and Registration (DruQuaR) group, Faculty of Pharmaceutical Sciences, Ghent University, Harelbekestraat 72, B-9000 Ghent, Belgium.
Sylvia Van DorpeDrug Quality and Registration (DruQuaR) group, Faculty of Pharmaceutical Sciences, Ghent University, Harelbekestraat 72, B-9000 Ghent, Belgium.
Evelien WynendaeleDrug Quality and Registration (DruQuaR) group, Faculty of Pharmaceutical Sciences, Ghent University, Harelbekestraat 72, B-9000 Ghent, Belgium.
Kathelijne PeremansDepartments of Medical Imaging and Physiology, Faculty of Veterinary Medicine, Ghent University, Salisburylaan 133, B9820 Merelbeke, Belgium.
Christian BurvenichDepartments of Medical Imaging and Physiology, Faculty of Veterinary Medicine, Ghent University, Salisburylaan 133, B9820 Merelbeke, Belgium.
Bart De SpiegeleerDrug Quality and Registration (DruQuaR) group, Faculty of Pharmaceutical Sciences, Ghent University, Harelbekestraat 72, B-9000 Ghent, Belgium.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Different fused-core stationary phase chemistries (C18, Amide, Phenyl-hexyl and Peptide ES-C18) were used for the analysis of 21 structurally representative model peptides. In addition, the effects of the mobile phase composition (ACN or MeOH as organic modifier; formic acid or acetic acid, as acidifying component) on the column selectivity, peak shape and overall chromatographic performance were evaluated. The RP-amide column, combined with a formic acid-acetonitrile based gradient system, performed as best. A peptide reversed-phase retention model is proposed, consisting of 5 variables: log SumAA, log Sv, clog P, log nHDon and log nHAcc. Quantitative structure-retention relationship (QSRR) models were constructed for 16 different chromatographic systems. The accuracy of this peptide retention model was demonstrated by the comparison between predicted and experimentally obtained retention times, explaining on average 86% of the variability. Moreover, using an external set of 5 validation peptides, the predictive power of the model was also demonstrated. This peptide retention model includes the novel

Indexed as

Fused-core (core-shell, core-enhanced, poro-shell, HALO®) stationary phasesIn-silico amino acid descriptorPeptidesRP-HPLC peptide retention model

Identifiers

PMID29403802
PMCPMC5760978

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.