Evidence map›Paper›PMID 42493465›Full record

ArticleJournal of mass spectrometry : JMS2026

Application of 2D-Chromatography System for the Determination of Cosmetic Peptides in Skin Homogenates.

Fosca Errante, Marco Pallecchi, Marta Menicatti, Lisa Giovannelli, Paolo Rovero, Gianluca Bartolucci

Abstract read
In one paragraph

Article in Journal of mass spectrometry : JMS, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

6 authors.

Fosca ErranteDepartment of Neurofarba (Department of Neurosciences, Psychology, Drug Research and Child Health), University of Florence, Florence, Italy.ORCID https://orcid.org/0000-0001-7790-9886
Marco PallecchiDepartment of Neurofarba (Department of Neurosciences, Psychology, Drug Research and Child Health), University of Florence, Florence, Italy.ORCID https://orcid.org/0000-0002-0057-6531
Marta MenicattiDepartment of Neurofarba (Department of Neurosciences, Psychology, Drug Research and Child Health), University of Florence, Florence, Italy.ORCID https://orcid.org/0000-0001-8302-7644
Lisa GiovannelliDepartment of Neurofarba (Department of Neurosciences, Psychology, Drug Research and Child Health), University of Florence, Florence, Italy.ORCID https://orcid.org/0000-0002-4027-4693
Paolo RoveroDepartment of Neurofarba (Department of Neurosciences, Psychology, Drug Research and Child Health), University of Florence, Florence, Italy.ORCID https://orcid.org/0000-0001-9577-5228
Gianluca BartolucciDepartment of Neurofarba (Department of Neurosciences, Psychology, Drug Research and Child Health), University of Florence, Florence, Italy.ORCID https://orcid.org/0000-0002-5631-8769

Funding

Regione Toscana PORCREO FESR 2007-2013
6 · The paper itself

Abstract

Peptides are increasingly employed as active ingredients in both therapeutic and cosmeceutical applications due to their high biological specificity, favorable safety profiles, and expanding market relevance. In topical formulations, peptide activity is typically confined to the skin, where widespread dermal proteases may significantly affect their stability and efficacy. Despite the growing use of bioactive peptides in dermatological and cosmeceutical products, robust analytical methodologies for assessing their susceptibility to dermal enzymatic degradation remain limited. In this study, a two-dimensional HPLC-MS/MS (2D-HPLC-MS/MS) method based on ion trap detection was developed and validated for the quantitative evaluation of peptide stability in human skin homogenate (HSH). The analytical setup integrates online cleanup with chromatographic separation on a silica-based pentafluorophenyl (PFP) column, enabling reliable analysis of peptides with different polarity profiles within a single workflow. The system enables direct injection of sample solutions with relatively high organic solvent content, allowing limited sample dilution and preservation of analytical sensitivity. A key feature of the method is the use of isomeric peptide analogues as internal standards, monitored under identical MS/MS conditions as their corresponding analytes. This approach provides effective correction for ionization and fragmentation variability while offering a practical alternative to stable isotope-labelled standards. The ion trap mass analyzer ensured controlled and reproducible fragmentation behavior, supporting robust quantitative performance. The developed method demonstrated satisfactory linearity, sensitivity, precision, accuracy, and minimal matrix effects. Application to stability studies of three peptides with distinct polarity profiles confirmed its suitability for monitoring degradation kinetics in HSH. Overall, this 2D-HPLC-MS/MS strategy provides a versatile analytical platform for dermal peptide stability assessment and supports early-stage screening and preclinical studies of bioactive peptides intended for topical applications.

Indexed as

CosmeticsLiquid Chromatography-Mass SpectrometryPeptidesSkinTandem Mass SpectrometryChromatography, High Pressure LiquidHumansReproducibility of ResultsCosmeticsPeptidesdermal stabilityion trap mass spectrometryisomeric peptide analoguesonline sample cleanupscrambled peptide

Identifiers

PMID42493465
PMCPMC13395628

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Registered trials

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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.