Self-assembly of super-hydrophobic PMMA microspheres on silicon wafer as MALDI-MS chip for rapid quantification of peptides
•A novel super-hydrophobic structured-PMMA chip for MALDI-MS is prepared by a simple self-assembly method.•The MALDI-MS detection reproducibility and sensitivity are highly improved with this chip compared to the conventional steel target.•Different peptides can be quantified in a broad range with t...
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Published in | Sensors and actuators. B, Chemical Vol. 306; p. 127573 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
Lausanne
Elsevier B.V
01.03.2020
Elsevier Science Ltd |
Subjects | |
Online Access | Get full text |
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Summary: | •A novel super-hydrophobic structured-PMMA chip for MALDI-MS is prepared by a simple self-assembly method.•The MALDI-MS detection reproducibility and sensitivity are highly improved with this chip compared to the conventional steel target.•Different peptides can be quantified in a broad range with this chip by MALDI-MS without internal standard.•Different practical peptides samples can be quantified in a broad range with this chip without internal standard by MALDI-MS.
Rapid quantification of peptides by matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) is a challenge. Herein, we prepared a super-hydrophobic poly(methyl methacrylate) (PMMA) structured chip for quantifying peptides without internal standard by improving the detection reproducibility and sensitivity. The chip was formed by PMMA microspheres through a self-assembly method. As a good adsorbent of peptides, PMMA microspheres make peptides distributed uniformly on the chip, resulting in the elimination of the coffee ring effect and the homogeneous co-crystallization of peptides/matrix. The relative standard deviations (∼ 10 %) and coefficients of determination (∼ 0.99) are satisfactory when detecting 3 standard peptides, which show that the chip is applicable for rapid quantification of peptides. The limit of detection is improved by 1000-fold on this chip compared with conventional steel target because of the enrichment of the super-hydrophobicity. It can be concluded that the detection reproducibility and sensitivity are significantly improved by the super-hydrophobic structured-PMMA chip. The applicability of the chip for practical samples is demonstrated by quantifying bacitracin A in milk extract and bradykinin1-7 in serum with good linearities. The structured-PMMA chips exhibit competitive advantages for quantitative analysis of peptides, which have a great potential for proteomic research. |
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ISSN: | 0925-4005 1873-3077 |
DOI: | 10.1016/j.snb.2019.127573 |