Effect of shell structure of Ti-immobilized metal ion affinity chromatography core-shell magnetic particles for phosphopeptide enrichment Article Swipe
Anna Laura Capriotti
,
Michela Antonelli
,
Diego Antonioli
,
Chiara Cavaliere
,
Riccardo Chiarcos
,
Valentina Gianotti
,
Susy Piovesana
,
Katia Sparnacci
,
Michele Laus
,
Aldo Laganà
·
YOU?
·
· 2019
· Open Access
·
· DOI: https://doi.org/10.1038/s41598-019-51995-z
YOU?
·
· 2019
· Open Access
·
· DOI: https://doi.org/10.1038/s41598-019-51995-z
Magnetic materials in sample preparation for shotgun phosphoproteomics offer several advantages over conventional systems, as the enrichment can be achieved directly in solution, but they still suffer from some drawbacks, due to limited stability and selectivity, which is supposed to be affected by the hydrophilicity of the polymeric supports used for cation immobilization. The paper describes the development of an improved magnetic material with increased stability, thanks to a two-step covering of the magnetic core, for the enrichment of phosphopeptides in biological samples. Four materials were prepared featuring a polymeric shell with tunable hydrophilicity, obtained by “grafting from” polymerization of glycidyl methacrylate with 0–8.3% of polyethylene glycol methacrylate (PEGMA), the latter used to modulate the hydrophilicity of the material surface. Finally, the materials were functionalized with iminodiacetic acid for Ti 4+ ion immobilization. The materials were analyzed for their composition by a combination of CHN elemental analysis and thermogravimetric analysis, also hyphenated to gas chromatography and mass spectrometric detection. Surface characteristics were evaluated by water contact angle measurements, scanning electron microscopy and energy dispersive X-ray spectrometry. These materials were applied to the enrichment of phosphopeptides from yeast protein digests. Peptides were identified by proteomics techniques using nano-high performance liquid chromatography coupled to mass spectrometry and bioinformatics. Qualitatively the peptides identified by the four systems were comparable, with 1606–1693 phosphopeptide identifications and a selectivity of 47–54% for all materials. The physico-chemical features of the identified peptides were also the same for the four materials. In particular, the grand average of hydropathy index values indicated that the enriched phosphopeptides were hydrophilic (ca. 90%), and only some co-enriched non-phosphorylated peptides were hydrophobic (21–28%), regardless of the material used for enrichment. Peptides had a pI ≤ 7, which indicated a well-known bias for acidic peptides binding, attributed to the interaction with the metal center itself. The results indicated that the enrichment of phosphopeptides and the co-enrichment of non-phosphorylated peptides is mainly driven by interactions with Ti 4+ and does not depend on the amount of PEGMA chains in the polymer shell.
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- Type
- article
- Language
- en
- Landing Page
- https://doi.org/10.1038/s41598-019-51995-z
- https://www.nature.com/articles/s41598-019-51995-z.pdf
- OA Status
- gold
- Cited By
- 8
- References
- 48
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W2982508989
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
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https://openalex.org/W2982508989Canonical identifier for this work in OpenAlex
- DOI
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https://doi.org/10.1038/s41598-019-51995-zDigital Object Identifier
- Title
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Effect of shell structure of Ti-immobilized metal ion affinity chromatography core-shell magnetic particles for phosphopeptide enrichmentWork title
- Type
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articleOpenAlex work type
- Language
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enPrimary language
- Publication year
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2019Year of publication
- Publication date
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2019-10-31Full publication date if available
- Authors
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Anna Laura Capriotti, Michela Antonelli, Diego Antonioli, Chiara Cavaliere, Riccardo Chiarcos, Valentina Gianotti, Susy Piovesana, Katia Sparnacci, Michele Laus, Aldo LaganàList of authors in order
- Landing page
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https://doi.org/10.1038/s41598-019-51995-zPublisher landing page
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https://www.nature.com/articles/s41598-019-51995-z.pdfDirect link to full text PDF
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YesWhether a free full text is available
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goldOpen access status per OpenAlex
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https://www.nature.com/articles/s41598-019-51995-z.pdfDirect OA link when available
- Concepts
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Phosphopeptide, Shell (structure), Chemistry, Metal, Chromatography, Materials science, Chemical engineering, Peptide, Biochemistry, Organic chemistry, Engineering, Composite materialTop concepts (fields/topics) attached by OpenAlex
- Cited by
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8Total citation count in OpenAlex
- Citations by year (recent)
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2025: 1, 2023: 1, 2022: 1, 2021: 4, 2020: 1Per-year citation counts (last 5 years)
- References (count)
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48Number of works referenced by this work
- Related works (count)
-
10Other works algorithmically related by OpenAlex
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| abstract_inverted_index.proteomics | 194 |
| abstract_inverted_index.regardless | 271 |
| abstract_inverted_index.stability, | 66 |
| abstract_inverted_index.techniques | 195 |
| abstract_inverted_index.well-known | 287 |
| abstract_inverted_index.(21–28%), | 270 |
| abstract_inverted_index.1606–1693 | 218 |
| abstract_inverted_index.co-enriched | 265 |
| abstract_inverted_index.combination | 143 |
| abstract_inverted_index.comparable, | 216 |
| abstract_inverted_index.composition | 140 |
| abstract_inverted_index.development | 58 |
| abstract_inverted_index.enrichment. | 277 |
| abstract_inverted_index.hydrophilic | 259 |
| abstract_inverted_index.hydrophobic | 269 |
| abstract_inverted_index.interaction | 296 |
| abstract_inverted_index.particular, | 245 |
| abstract_inverted_index.performance | 198 |
| abstract_inverted_index.preparation | 5 |
| abstract_inverted_index.selectivity | 223 |
| abstract_inverted_index.“grafting | 97 |
| abstract_inverted_index.conventional | 13 |
| abstract_inverted_index.interactions | 320 |
| abstract_inverted_index.methacrylate | 102, 108 |
| abstract_inverted_index.polyethylene | 106 |
| abstract_inverted_index.selectivity, | 36 |
| abstract_inverted_index.spectrometry | 204 |
| abstract_inverted_index.Qualitatively | 207 |
| abstract_inverted_index.co-enrichment | 312 |
| abstract_inverted_index.iminodiacetic | 127 |
| abstract_inverted_index.measurements, | 168 |
| abstract_inverted_index.spectrometric | 158 |
| abstract_inverted_index.spectrometry. | 176 |
| abstract_inverted_index.chromatography | 155, 200 |
| abstract_inverted_index.functionalized | 125 |
| abstract_inverted_index.hydrophilicity | 45, 116 |
| abstract_inverted_index.phosphopeptide | 219 |
| abstract_inverted_index.polymerization | 99 |
| abstract_inverted_index.bioinformatics. | 206 |
| abstract_inverted_index.characteristics | 161 |
| abstract_inverted_index.hydrophilicity, | 94 |
| abstract_inverted_index.identifications | 220 |
| abstract_inverted_index.immobilization. | 53, 133 |
| abstract_inverted_index.phosphopeptides | 80, 185, 257, 309 |
| abstract_inverted_index.physico-chemical | 230 |
| abstract_inverted_index.phosphoproteomics | 8 |
| abstract_inverted_index.thermogravimetric | 149 |
| abstract_inverted_index.non-phosphorylated | 266, 314 |
| cited_by_percentile_year.max | 97 |
| cited_by_percentile_year.min | 89 |
| countries_distinct_count | 1 |
| institutions_distinct_count | 10 |
| citation_normalized_percentile.value | 0.67116127 |
| citation_normalized_percentile.is_in_top_1_percent | False |
| citation_normalized_percentile.is_in_top_10_percent | False |