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Tryp-N: A thermostable protease for the production of N-terminal argininyl and lysinyl peptides

ABSTRACT: Identification and characterization of Tryp-N, A thermostable protease for the production of N-terminal argininyl and lysinyl peptides

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Embryo, Permanent Cell Line Cell, Kidney

SUBMITTER: Jonathan Ipsaro

LAB HEAD: Darryl J. Pappin

PROVIDER: PXD017030 | Pride | 2020-04-22

REPOSITORIES: Pride

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			Action	DRS
	TrypN_replicate1.dat	Other
	TrypN_replicate1_Fx_1.raw	Raw
	TrypN_replicate1_Fx_2.raw	Raw
	TrypN_replicate1_Fx_3.raw	Raw
	TrypN_replicate1_Fx_4.raw	Raw

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Publications

Tryp-N: A Thermostable Protease for the Production of N-terminal Argininyl and Lysinyl Peptides.

Wilson John P JP Ipsaro Jonathan J JJ Del Giudice Samantha N SN Turna Nikita Saha NS Gauss Carla M CM Dusenbury Katharine H KH Marquart Krisann K Rivera Keith D KD Pappin Darryl J DJ

Journal of proteome research 20200320 4

Bottom-up proteomics is a mainstay in protein identification and analysis. These studies typically employ proteolytic treatment of biological samples to generate suitably sized peptides for tandem mass spectrometric (MS) analysis. In MS, fragmentation of peptides is largely driven by charge localization. Consequently, peptides with basic centers exclusively on their N-termini produce mainly b-ions. Thus, it was long ago realized that proteases that yield such peptides would be valuable proteomic ...[more]

PMID: 32141294

Similar Datasets

Tryp-N: A thermostable protease for the production of N-terminal argininyl and lysinyl peptides

Project description:Identification and characterization of Tryp-N, A thermostable protease for the production of N-terminal argininyl and lysinyl peptides

2020-04-22 | PXD017023 | Pride

Tryp-N: A thermostable protease for the production of N-terminal argininyl and lysinyl peptides

Project description:Identification and characterization of Tryp-N, A thermostable protease for the production of N-terminal argininyl and lysinyl peptides

2020-04-22 | PXD017024 | Pride

Tryp-N: A thermostable protease for the production of N-terminal argininyl and lysinyl peptides

Project description:Identification and characterization of Tryp-N, A thermostable protease for the production of N-terminal argininyl and lysinyl peptides

2020-04-22 | PXD017021 | Pride

Tryp-N: A thermostable protease for the production of N-terminal argininyl and lysinyl peptides

Project description:Identification and characterization of Tryp-N, A thermostable protease for the production of N-terminal argininyl and lysinyl peptides

2020-04-22 | PXD017048 | Pride

Tryp-N: A Thermostable Protease for the Production of N-terminal Argininyl and Lysinyl Peptides.

Project description:Bottom-up proteomics is a mainstay in protein identification and analysis. These studies typically employ proteolytic treatment of biological samples to generate suitably sized peptides for tandem mass spectrometric (MS) analysis. In MS, fragmentation of peptides is largely driven by charge localization. Consequently, peptides with basic centers exclusively on their N-termini produce mainly b-ions. Thus, it was long ago realized that proteases that yield such peptides would be valuable proteomic tools for achieving simplified peptide fragmentation patterns and peptide assignment. Work by several groups has identified such proteases, however, structural analysis of these suggested that enzymatic optimization was possible. We therefore endeavored to find enzymes that could provide enhanced activity and versatility while maintaining specificity. Using these previously described proteases as informatic search templates, we discovered and then characterized a thermophilic metalloprotease with N-terminal specificity for arginine and lysine. This enzyme, dubbed Tryp-N, affords many advantages including improved thermostability, solvent and detergent tolerance, and rapid digestion time.

| S-EPMC7842235 | biostudies-literature

Introducing synthetic thermostable RNase inhibitors in single-cell RNA-seq

Project description:Single-cell RNA-sequencing (scRNAseq) is revolutionizing biomedicine, propelled by advances in methodology, ease of use, and cost reduction of library preparation. Over the past decade, there have been remarkable technical improvements in most aspects of single-cell transcriptomics. Yet, there has been little to no progress in advancing RNase inhibition despite that maintained RNA integrity is critical during cell collection, storage, and cDNA library generation. Here, we demonstrate that a synthetic thermostable RNase inhibitor yield single-cell libraries of equal or superior quality compared to ubiquitously used protein-based recombinant RNase inhibitors (RRIs). Importantly, the synthetic RNase inhibitor provide additional unique improvements in reproducibility and throughput, enable new experimental workflows including heat cycles, and can reduce the need for dry-ice transports. In summary, replacing RRIs represents a substantial advancement in the field of single-cell transcriptomics.

2024-07-29 | E-MTAB-13873 | biostudies-arrayexpress

Introducing synthetic thermostable RNase inhibitors in single-cell RNA-seq (Bulk RNA-seq libraries)

2024-07-26 | E-MTAB-13899 | biostudies-arrayexpress

Potato protein hydrolysate LC-MS/MS

Project description:Peptides and protein hydrolysates are promising alternatives to substitute chemical additives as functional food ingredients. In this study, we present a novel approach for producing a potato protein hydrolysate with improved emulsifying and foaming properties by data-driven, targeted hydrolysis. Based on previous studies, we selected 15 emulsifier peptides derived from abundant potato proteins, which were clustered based on sequence identity. Through in silico analysis, we determined that from a range of industrial proteases (Neutrase (Neut), Alcalase (Alc), Flavorzyme (Flav) and Trypsin (Tryp)), Tryp was found more likely to release peptides resembling the target peptides. After applying all proteases individually, hydrolysates were assayed for in vitro emulsifying and foaming properties. No direct correlation between degree of hydrolysis and interfacial properties was found. Tryp produced a hydrolysate (DH=5.4%) with the highest (P<0.05) emulsifying and foaming abilities, good stabilities, and high aqueous solubility. Using LC-MS/MS, we identified >10,000 peptides in each hydrolysate. Through peptide mapping, we show that random overlapping with known peptide emulsifiers is not sufficient to quantitatively describe hydrolysate functionality. While Neut hydrolysates had the highest proportion of peptides with target overlap, they showed inferior interfacial activity. In contrast, Tryp was able to release specifically targeted peptides, explaining the high surface activity observed. While modest yields and residual unhydrolyzed protein indicate room for process improvement, this work shows that data-driven, targeted hydrolysis is a viable, interdisciplinary approach to facilitate hydrolysis design for production of functional hydrolysates from alternative protein sources.

2024-03-04 | PXD034139 | Pride

Crosslinking experiment of the RAGE-S100B complex

Project description:XL-MS of RAGE-100B complex. The Crosslinking agent is BS3. Samples were subjected to sequential digestion. 91212_AM_2_2_1_HCDFT, 91212_AM_2_2_2_HCDFT, 91212_AM_5_2_2_HCDFT, 91212_AM_5_2_2_HCDFT - Tryp-Chym; 91212_AM_2_3_1_HCDFT, 91212_AM_2_3_2_HCDFT, 91212_AM_5_3_2_HCDFT, 91212_AM_5_3_2_HCDFT - Tryp-Gluc; 91212_AM_2_1_1_HCDFT, 91212_AM_2_1_2_HCDFT, 91212_AM_5_1_2_HCDFT, 91212_AM_5_1_2_HCDFT - Tryp-Tryp.

2020-11-11 | MSV000086437 | MassIVE

Crosslinking experiment of the RAGE oligomeric complexes

Project description:XL-MS of RAGE oligomeric complexes. The Crosslinking agent is BS3. Samples were subjected to sequential digestion. 91212_AM_1_3_1_HCDFT, 91212_AM_1_3_2_HCDFT, 91212_AM_4_3_1_HCDFT, 91212_AM_4_3_2_HCDFT - Tryp-Gluc; 91212_AM_1_2_1_HCDFT, 91212_AM_1_2_2_HCDFT, 91212_AM_4_2_1_HCDFT, 91212_AM_4_2_2_HCDFT - Tryp-Chym; 91212_AM_1_1_1_HCDFT, 91212_AM_1_1_2_HCDFT, 91212_AM_4_1_1_HCDFT, 91212_AM_4_1_2_HCDFT - Tryp-Tryp.

2020-11-11 | MSV000086438 | MassIVE

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