Urea-Based Imprinted Polymer Hosts with Switchable Anion Preference

Shinde, Sudhirkumar; Incel, Anil; Mansour, Mona; Olsson, Gustaf D.; Nicholls, Ian A.; Esen, Cem; Urraca, Javier; Sellergren, Börje

doi:10.1021/jacs.0c00707

Cited by 38 publications

(34 citation statements)

References 74 publications

(157 reference statements)

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“…This was covered in depth in our previous report. 43 The nature of the counter-cation has been shown to strongly influence the template-monomer complexation and in turn the target affinity exerted by the MIP. Enhanced complex stability is obtained by the use of quaternary ammonium ions like tetrabutylammonium (TBA), also accompanied by pronounced counterion memory effects.…”

Section: Resultsmentioning

confidence: 99%

Selective Enrichment of Histidine Phosphorylated Peptides Using Molecularly Imprinted Polymers

et al. 2021

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Protein histidine phosphorylation (pHis) is involved in molecular signaling networks in bacteria, fungi, plants, and higher eukaryotes including mammals and is implicated in human diseases such as cancer. Detailed investigations of the pHis modification are hampered due to its acid-labile nature and consequent lack of tools to study this post-translational modification (PTM). We here demonstrate three molecularly imprinted polymer (MIP)-based reagents, MIP1–MIP3, for enrichment of pHis peptides and subsequent characterization by chromatography and mass spectrometry (LC–MS). The combination of MIP1 and β-elimination provided some selectivity for improved detection of pHis peptides. MIP2 was amenable to larger pHis peptides, although with poor selectivity. Microsphere-based MIP3 exhibited improved selectivity and was amenable to enrichment and detection by LC–MS of pHis peptides in tryptic digests of protein mixtures. These MIP protocols do not involve any acidic solvents during sample preparation and enrichment, thus preserving the pHis modification. The presented proof-of-concept results will lead to new protocols for highly selective enrichment of labile protein phosphorylations using molecularly imprinted materials.

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Section: Resultsmentioning

confidence: 99%

Selective Enrichment of Histidine Phosphorylated Peptides Using Molecularly Imprinted Polymers

et al. 2021

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“…Although it could not be introduced due to space limitations, the ureido group is also used as an important functional group in research such as polymer-based hosts, metal-organic frameworks (MOF) andc ovalento rganic frameworks (COF), as well as molecularm achines. [170][171][172][173][174] Urea is the oldest artificial organic molecule, but even today,c ompounds with interesting functions have been continuously emerging from its derivatives.…”

Section: Discussionmentioning

confidence: 99%

“…In recent years, the concept of molecular recognition has been positively applied to catalyst design, and various useful reactions catalyzed by ureido molecules have been developed. Although it could not be introduced due to space limitations, the ureido group is also used as an important functional group in research such as polymer‐based hosts, metal–organic frameworks (MOF) and covalent organic frameworks (COF), as well as molecular machines [170–174] . Urea is the oldest artificial organic molecule, but even today, compounds with interesting functions have been continuously emerging from its derivatives.…”

Section: Discussionmentioning

confidence: 99%

Urea Derivatives as Functional Molecules: Supramolecular Capsules, Supramolecular Polymers, Supramolecular Gels, Artificial Hosts, and Catalysts

Yokoya

Kimura

Yamanaka

2021

Chemistry A European J

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Urea, which has both hydrogen bond acceptor and donor moieties, is an ideal structuref or as upramolecular synthon. Various supramolecules having ureido group(s) have been widelyd eveloped. This article summarizes recent developments of urea derivatives that exhibit various functions:i)supramolecular capsules that form discreteu reaurea intermolecular hydrogen bonds, ii)supramolecular polymers that form continuous urea-urea intermolecularh ydrogen bonds, iii)supramolecular gels that form continuous urea-urea intermolecular hydrogen bonds, iv) artificialh ost molecules based on the molecular recognition ability of the ureido group, and v) catalytic reactions developedb yu tilizing the molecular recognition ability of the ureido group.

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“…In addition to the technological advancements, the preparation of pMIPs is expected to take great benefits from the available bioinformatics protein-addressed resources. The crosstalk between polymer chemists, synthetic chemists devoted to the design of specific monomers for defined interactions, such as phospho-recognition [95,96], protein structurists, and bioinformatics, is foreseen as the key to enable the formation of selective pMIP binding sites that will perform the unique recognition towards the target protein, also in extremely harsh biological conditions, such as the high degree complexity of the protein landscape in vivo.…”

Section: Discussionmentioning

confidence: 99%

Molecularly imprinted polymers by epitope imprinting: a journey from molecular interactions to the available bioinformatics resources to scout for epitope templates

Pasquardini¹,

Bossi

2021

Anal Bioanal Chem

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The molecular imprinting of proteins is the process of forming biomimetics with entailed protein-recognition by means of a template-assisted synthesis. Protein-imprinted polymers (pMIPs) have been successfully employed in separations, assays, sensors, and imaging. From a technical point of view, imprinting a protein is both costly, for protein expression and purification, and challenging, for the preservation of the protein’s structural properties. In fact, the imprinting process needs to guarantee the preservation of the same protein three-dimensional conformation that later would be recognized. So far, the captivating idea to imprint just a portion of the protein, i.e., an epitope, instead of the whole, proved successful, offering reduced costs, compatibility with many synthetic conditions (solvents, pH, temperatures), and fine-tuning of the peptide sequence so to target specific physiological and functional conditions of the protein, such as post-translational modifications. Here, protein-protein interactions and the biochemical features of the epitopes are inspected, deriving lessons to prepare more effective pMIPs. Epitopes are categorized in linear or structured, immunogenic or not, located at the protein’s surface or buried in its core and the imprinting strategies are discussed. Moreover, attention is given to freely available online bioinformatics resources that might offer key tools to gain further rationale amid the selection process of suitable epitopes templates.

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Urea-Based Imprinted Polymer Hosts with Switchable Anion Preference

Cited by 38 publications

References 74 publications

Selective Enrichment of Histidine Phosphorylated Peptides Using Molecularly Imprinted Polymers

Selective Enrichment of Histidine Phosphorylated Peptides Using Molecularly Imprinted Polymers

Urea Derivatives as Functional Molecules: Supramolecular Capsules, Supramolecular Polymers, Supramolecular Gels, Artificial Hosts, and Catalysts

Molecularly imprinted polymers by epitope imprinting: a journey from molecular interactions to the available bioinformatics resources to scout for epitope templates

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