Influence of Bead Chemistry and Protein-to-Bead Ratio on the Efficiency of Solid-Phase Proteolysis

Single-pot, solid-phase-enhanced sample preparation (SP3) is a rapid, automatable, and cost-effective protein cleanup technique facilitated by the aggregation and digestion of proteins on paramagnetic beads. In this study, we document how plasma protein-to-bead ratio influences the performance in terms of the number of identified peptides and proteins for two chemically modified paramagnetic SP3 beads, i.e., Carboxylate-Speedbeads and MagReSyn-Hydroxyl beads. The optimized protein-to-bead ratio enabled the identification of 17% more plasma protein groups than the nonoptimized condition. Furthermore, we evidenced differences in the quantification results of peptides upon aggregation on hydroxyl- and carboxylate-modified beads. By assessing the physicochemical properties of these peptides, significant differences were revealed in their pI values, charge, polarity, and aspartic and glutamic acid composition. Our results highlight that the choice of beads and protein-to-bead ratio are two important parameters that require optimization depending on the physicochemical properties of the targeted proteins.

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Publication Details

Journal
Journal of Proteome Research
Published
2026-01-06
DOI
https://doi.org/10.1021/acs.jproteome.5c00630
Citations
1
Primary Topic
Advanced Proteomics Techniques and Applications
Type
article
Field-Weighted Citation Impact
16.26
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article

Influence of Bead Chemistry and Protein-to-Bead Ratio on the Efficiency of Solid-Phase Proteolysis

Jean Armengaud, Clément Lozano, Salem Al Siblani
1 citations
Journal of Proteome Research
Advanced Proteomics Techniques and Applications
16.26
article

Influence of Bead Chemistry and Protein-to-Bead Ratio on the Efficiency of Solid-Phase Proteolysis

Jean Armengaud, Clément Lozano, Salem Al Siblani
article en
1 citations

Abstract

Single-pot, solid-phase-enhanced sample preparation (SP3) is a rapid, automatable, and cost-effective protein cleanup technique facilitated by the aggregation and digestion of proteins on paramagnetic beads. In this study, we document how plasma protein-to-bead ratio influences the performance in terms of the number of identified peptides and proteins for two chemically modified paramagnetic SP3 beads, i.e., Carboxylate-Speedbeads and MagReSyn-Hydroxyl beads. The optimized protein-to-bead ratio enabled the identification of 17% more plasma protein groups than the nonoptimized condition. Furthermore, we evidenced differences in the quantification results of peptides upon aggregation on hydroxyl- and carboxylate-modified beads. By assessing the physicochemical properties of these peptides, significant differences were revealed in their pI values, charge, polarity, and aspartic and glutamic acid composition. Our results highlight that the choice of beads and protein-to-bead ratio are two important parameters that require optimization depending on the physicochemical properties of the targeted proteins.

Journal of Proteome ResearchVol. 25(2)
Université de Montpellier (FR), Commissariat à l'Énergie Atomique et aux Énergies Alternatives (FR), Université Paris-Saclay (FR), Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement (FR), Laboratoire Innovations Technologiques pour la Détection et le Diagnostic (FR), Technologies pour la Santé (FR), CEA Paris-Saclay (FR)
Industry, innovation and infrastructure
Openalex Percentile: Top 4%
Advanced Proteomics Techniques and Applications
16.26
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