Evaluation of affinity-based serum clean-up in mass spectrometric analysis: Plastic vs monoclonal antibodies

Rossetti, Cecilia; Levernæs, Maren Christin Stillesby; Reubsaet, Léon; Halvorsen, Trine Grønhaug

doi:10.1016/j.chroma.2016.09.069

Cited by 16 publications

(29 citation statements)

References 26 publications

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“…An application of great interest for tryptic peptide selective MIPs is the integration in diagnostic assays for severe diseases such as the aggressive tumor Small Cell Lung Cancer (SCLC) [36][37] (manuscript submitted).…”

Section: Introducionmentioning

confidence: 99%

“…Due to the wide protein concentration range in serum and, at the same time, to the limited dynamic range of the mass spectrometer, the selectivity of the MIP becomes a crucial factor to be evaluated and emphasized by the experimental conditions. The analysis of the species co-extracted with NLLGLIEAK in the MIP cartridge allowed the identification of many peptides belonging to serum albumin 37 , but limited information was achieved about the interactions playing fundamental roles in peptide retention.…”

Section: Introducionmentioning

confidence: 99%

“…The use of BSA as model protein was driven from its simplicity of digest, purchase and its revised annotation in UniProt database. Moreover serum albumin is the most abundant protein in serum, the matrix of choice for the detection of ProGRP, and a recent study showed strong albumin retention on a MIP cartridge developed for the quantification of ProGRP in serum37 . Hence the use of BSA as model system would mimic the human serum albumin in patient samples and hopefully would result in valuable information about the albumin peptides observed previously[37].…”

mentioning

confidence: 99%

“…Moreover serum albumin is the most abundant protein in serum, the matrix of choice for the detection of ProGRP, and a recent study showed strong albumin retention on a MIP cartridge developed for the quantification of ProGRP in serum37 . Hence the use of BSA as model system would mimic the human serum albumin in patient samples and hopefully would result in valuable information about the albumin peptides observed previously[37]. Thus a sequential elution with increasing organic solvent strength was performed using the target peptide NLLGLIEA[K_ 13 C6 15 N2] and the peptides coming from the digestion of BSA 48 mM, which allowed good MS signal intensities without cartridge overload.…”

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confidence: 99%

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Exploring the peptide retention mechanism in molecularly imprinted polymers

et al. 2017

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Molecularly imprinted polymers (MIPs) have been used as useful sorbents in solid-phase extraction for a wide range of molecules and sample matrices. Their unique selectivity can be fine-tuned in the imprinting process and is crucial for the extraction of macromolecules from complex matrices such as serum. A relevant example of this is the application of MIPs to peptides in diagnostic assays. In this article the selectivity of MIPs, previously implemented in a quantitative mass-spectrometric assay for the biomarker pro-gastrin-releasing peptide, is investigated. Partial least squares regression was used to generate models for the evaluation and prediction of the retention mechanism of MIPs. A hypothesis on interactions of MIPs with the target peptide was verified by ad hoc experiments considering the relevant peptide physicochemical properties highlighted from the multivariate analysis. Novel insights into and knowledge of the driving forces responsible for the MIP selectivity have been obtained and can be directly used for further optimization of MIP imprinting strategies. Graphical Abstract Applied analytical strategy: the Solid Phase Extraction (SPE) of digested Bovin Serum Albumin (BSA), using Molecularly Imprinted Polymers (MIP), is followed by the liquid chromatography-mass spectrometry (LC-MS) analysis for the identification of the retained peptides. The further application of multivariate analysis allows setting up a Partial Least Square (PLS) model, which describes the peptide retention into the MIP and gives additional knowledge to be used in the optimization of the MIP and the whole SPE method.

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Section: Introducionmentioning

confidence: 99%

Section: Introducionmentioning

confidence: 99%

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confidence: 99%

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Exploring the peptide retention mechanism in molecularly imprinted polymers

et al. 2017

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“…The LOD of this method was determined to be 17 pM and thus substantially lower than the limit achieved by a MIP‐based extraction of ProGRP reported earlier (625 pM) but was still marginally higher than that of the immunocapture LC–MS (1 pM) and time‐resolved immunofluorometric assay methods . The coupling of a MIP trap column with an analytical column and MS/MS detection allowed a fully automated determination of ProGRP levels in patient samples using a low sample volume (50 μL) and short analysis time represents a noteworthy advance in biomarker determination by LC–MS using synthetic receptors .…”

Section: Examples Of Molecularly Imprinted Polymers Applied For the Smentioning

confidence: 99%

Advances in the development of molecularly imprinted polymers for the separation and analysis of proteins with liquid chromatography

Boysen

2018

J of Separation Science

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This review documents recent advances in the design, synthesis, characterization, and application of molecularly imprinted polymers in the form of monoliths and particles/beads for the use in the separation and analysis of proteins with solid‐phase extraction or liquid chromatography. The merits of three‐dimensional molecular imprinting, whereby the molecular template is randomly embedded in the polymer, and two‐dimensional imprinting, in which the template is confined to the surface, are described. Target protein binding can be achieved by either using the entire protein as a template or by using a protein substructure as template, that is, a peptide, as in the "epitope" approach. The intended approach and strategy then determine the choice of polymerization method. A synopsis has been provided on methods used for the physical, chemical, and functional characterizations and associated performance evaluations of molecularly imprinted and nonimprinted control polymers, involving a diverse range of analytical techniques commonly used for low and high molecular mass analytes. Examples of recent applications demonstrate that, due to the versatility of imprinting methods, molecularly imprinted monoliths or particles/beads can be adapted to protein extraction/depletion and separation procedures relevant to, for example, protein biomarker detection and quantification in biomedical diagnostics and targeted proteomics.

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Sample Preparation for LC‐MS Bioanalysis of Peptides

Yuan¹

2019

Sample Preparation in LC‐MS Bioanalysis

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Evaluation of affinity-based serum clean-up in mass spectrometric analysis: Plastic vs monoclonal antibodies

Cited by 16 publications

References 26 publications

Exploring the peptide retention mechanism in molecularly imprinted polymers

Exploring the peptide retention mechanism in molecularly imprinted polymers

Advances in the development of molecularly imprinted polymers for the separation and analysis of proteins with liquid chromatography

Sample Preparation for LC‐MS Bioanalysis of Peptides

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