DMF-MALDI: droplet based microfluidic combined to MALDI-TOF for focused peptide detection

Abstract We present an automated droplet microfluidic system (DMF) to generate monitored nanoliter aqueous droplets in oil and their deposition on a commercial stainless steel plate for MALDI-TOF analysis of peptides or protein digests. We demonstrate that DMF-MALDI combination focuses the analyte o...

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Main Authors: Kiarach Mesbah, Robert Thai, Sarah Bregant, Florent Malloggi
Format: Article
Language:English
Published: Nature Publishing Group 2017-07-01
Series:Scientific Reports
Online Access:https://doi.org/10.1038/s41598-017-06660-8
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spelling doaj-e69f693adbf54fc9b48ca747cf076df12020-12-08T01:24:48ZengNature Publishing GroupScientific Reports2045-23222017-07-01711810.1038/s41598-017-06660-8DMF-MALDI: droplet based microfluidic combined to MALDI-TOF for focused peptide detectionKiarach Mesbah0Robert Thai1Sarah Bregant2Florent Malloggi3LIONS, NIMBE, CEA, CNRS, Université Paris-SaclaySIMOPRO, JOLIOT, DRF, CEA, Université Paris-SaclaySIMOPRO, JOLIOT, DRF, CEA, Université Paris-SaclayLIONS, NIMBE, CEA, CNRS, Université Paris-SaclayAbstract We present an automated droplet microfluidic system (DMF) to generate monitored nanoliter aqueous droplets in oil and their deposition on a commercial stainless steel plate for MALDI-TOF analysis of peptides or protein digests. We demonstrate that DMF-MALDI combination focuses the analyte on the MALDI plate, increasing considerably the homogeneity of the dried material. This results in a 30times enhanced MALDI-TOF MS signal for a model peptide, allowing a significant improvement of the detection sensitivity limit (down to few tens of attomoles). Moreover, positive detection can be achieved from sub-nanomolar peptides solutions and better overall protein sequence coverages are obtained from few tens attomoles of protein digest. These results make DMF-MALDI a promising approach for the treatment of peptides samples as well as a key component for an integrated approach in the proteomic field.https://doi.org/10.1038/s41598-017-06660-8
collection DOAJ
language English
format Article
sources DOAJ
author Kiarach Mesbah
Robert Thai
Sarah Bregant
Florent Malloggi
spellingShingle Kiarach Mesbah
Robert Thai
Sarah Bregant
Florent Malloggi
DMF-MALDI: droplet based microfluidic combined to MALDI-TOF for focused peptide detection
Scientific Reports
author_facet Kiarach Mesbah
Robert Thai
Sarah Bregant
Florent Malloggi
author_sort Kiarach Mesbah
title DMF-MALDI: droplet based microfluidic combined to MALDI-TOF for focused peptide detection
title_short DMF-MALDI: droplet based microfluidic combined to MALDI-TOF for focused peptide detection
title_full DMF-MALDI: droplet based microfluidic combined to MALDI-TOF for focused peptide detection
title_fullStr DMF-MALDI: droplet based microfluidic combined to MALDI-TOF for focused peptide detection
title_full_unstemmed DMF-MALDI: droplet based microfluidic combined to MALDI-TOF for focused peptide detection
title_sort dmf-maldi: droplet based microfluidic combined to maldi-tof for focused peptide detection
publisher Nature Publishing Group
series Scientific Reports
issn 2045-2322
publishDate 2017-07-01
description Abstract We present an automated droplet microfluidic system (DMF) to generate monitored nanoliter aqueous droplets in oil and their deposition on a commercial stainless steel plate for MALDI-TOF analysis of peptides or protein digests. We demonstrate that DMF-MALDI combination focuses the analyte on the MALDI plate, increasing considerably the homogeneity of the dried material. This results in a 30times enhanced MALDI-TOF MS signal for a model peptide, allowing a significant improvement of the detection sensitivity limit (down to few tens of attomoles). Moreover, positive detection can be achieved from sub-nanomolar peptides solutions and better overall protein sequence coverages are obtained from few tens attomoles of protein digest. These results make DMF-MALDI a promising approach for the treatment of peptides samples as well as a key component for an integrated approach in the proteomic field.
url https://doi.org/10.1038/s41598-017-06660-8
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