Antibody-free ultra-high performance liquid chromatography/tandem mass spectrometry measurement of angiotensin I and II using magnetic epitope-imprinted polymers

Tan, Lei; Yu, Zerong; Zhou, Xiaoming; Xing, Da; Liu, Xiang; Peng, Rongfei; Tang, Yawen

doi:10.1016/j.chroma.2015.07.114

Cited by 20 publications

(21 citation statements)

References 31 publications

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“…Therefore, this approach is well suited for imprinting of biomacromolecules like proteins . Depending on application modes, the solid supports subjected to surface imprinting of proteins can be nanomaterials , electrodes , microspheres , membranes , and monoliths. Molecular imprinting of proteins in polymers attached to the surface of nanomaterials is currently a hot topic; however, this application mainly focuses on the fabrication of biosensors since the nanomaterials exhibit a remarkably large surface‐to‐volume ratio and size‐related physical and chemical properties.…”

Section: Introductionmentioning

confidence: 99%

“Smart” molecularly imprinted monoliths for the selective capture and easy release of proteins

Wen

Tan

Sun

et al. 2016

J of Separation Science

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A new thermally switchable molecularly imprinted monolith for the selective capture and release of proteins has been designed. First, a generic poly(glycidyl methacrylate-co-ethylene dimethacrylate) monolith reacted with ethylenediamine followed by functionalization with 2-bromoisobutyryl bromide to introduce the initiator for atom transfer radical polymerization. Subsequently, a protein-imprinted poly(N-isopropylacrylamide) layer was grafted onto the surface of the monolithic matrix by atom transfer radical polymerization. Scanning electron microscopy and energy-dispersive X-ray spectroscopy of the cross-sections of imprinted monoliths confirmed the formation of dense poly(N-isopropylacrylamide) brushes on the pore surface. The imprinted monolith exhibited high specificity and selectivity toward its template protein myoglobin over competing proteins and a remarkably large maximum adsorption capacity of 1641 mg/g. Moreover, this "smart" imprinted monolith featured thermally responsive characteristics that enabled selective capture and easy release of proteins triggered only by change in temperature with water as the mobile phase and avoided use of stronger organic solvents or change in ionic strength and pH.

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Section: Introductionmentioning

confidence: 99%

“Smart” molecularly imprinted monoliths for the selective capture and easy release of proteins

Wen

Tan

Sun

et al. 2016

J of Separation Science

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“…This has to take in account many different interactions, simultaneously occurring around the template molecule, and the template insolubility into organic solvents generally used for the polymeric synthesis [26][27] . However, several MIPs have been developed for peptide enrichment and employed in the sample preparation of proteomic workflows [28][29][30][31][32][33][34][35] .…”

Section: Introducionmentioning

confidence: 99%

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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“…However, magnetic MIPs (mMIPs) are a promising emerging format that has shown some promise for the extraction of peptides present at low levels in serum. 12 …”

Section: Introductionmentioning

confidence: 99%

“… 21 Similarity, mMIPs have been shown to function in complex matrices: an mMIP targeting lysozyme demonstrated clear enrichment in egg white. 22 While an mMIP targeting the peptide hormones angiotensin I and II demonstrated the value of mMIPs for the enrichment and quantification of peptides using LC-MS/MS, 12 the use of mMIPs for target enrichment and cleanup in bottom-up proteomics has not yet been reported.…”

Section: Introductionmentioning

confidence: 99%

Magnetic Synthetic Receptors for Selective Clean-Up in Protein Biomarker Quantification

et al. 2020

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Biomarker analysis by mass spectrometry (MS) can allow for the rapid quantification of low abundant biomarkers. However, the complexity of human serum is a limiting factor in MS-based bioanalysis; therefore, novel biomarker enrichment strategies are of interest, particularly if the enrichment strategies are of low cost and are easy to use. One such strategy involves the use of molecularly imprinted polymers (MIPs) as synthetic receptors for biomarker enrichment. In the present study, a magnetic solid-phase extraction (mSPE) platform, based on magnetic MIP (mMIP) sorbents, is disclosed, for use in the MS-based quantification of proteins by the bottom-up approach. Progastrin releasing peptide (ProGRP), a low abundant and clinically sensitive biomarker for small cell lung cancer (SCLC), was used to exemplify the mSPE platform. Four different mMIPs were synthesized, and an mSPE method was developed and optimized for the extraction of low concentrations of tryptic peptides from human serum. The mSPE method enabled the selective extraction of the ProGRP signature peptide, the nonapeptide NLLGLIEAK, prior to quantification of the target via LC-MS/MS. Overall, the mSPE method demonstrated its potential as a low cost, rapid, and straightforward sample preparation method, with demonstrably strong binding, acceptable recoveries, and good compatibility with MS. mMIPs are a potential low-cost alternative to current clinical methods for biomarker analysis.

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Antibody-free ultra-high performance liquid chromatography/tandem mass spectrometry measurement of angiotensin I and II using magnetic epitope-imprinted polymers

Cited by 20 publications

References 31 publications

“Smart” molecularly imprinted monoliths for the selective capture and easy release of proteins

“Smart” molecularly imprinted monoliths for the selective capture and easy release of proteins

Exploring the peptide retention mechanism in molecularly imprinted polymers

Magnetic Synthetic Receptors for Selective Clean-Up in Protein Biomarker Quantification

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