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In Mesopore Protein Digestion: A New Forthcoming Strategy in Proteomics

The conventional protocols for in solution or in gel protein digestion require many steps and long reaction times. The use of trypsin immobilized onto solid supports has recently captured the attention of many research groups, because these systems can speed-up protein digestion significantly. The u...

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Detalles Bibliográficos
Autores principales: Savino, Rocco, Casadonte, Francesca, Terracciano, Rosa
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6264412/
https://www.ncbi.nlm.nih.gov/pubmed/21765391
http://dx.doi.org/10.3390/molecules16075938
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author Savino, Rocco
Casadonte, Francesca
Terracciano, Rosa
author_facet Savino, Rocco
Casadonte, Francesca
Terracciano, Rosa
author_sort Savino, Rocco
collection PubMed
description The conventional protocols for in solution or in gel protein digestion require many steps and long reaction times. The use of trypsin immobilized onto solid supports has recently captured the attention of many research groups, because these systems can speed-up protein digestion significantly. The utilization of new materials such as mesoporous silica as supports, in which enzyme and substrate are dramatically concentrated and confined in the nanospace, offers new opportunities to reduce the complexity of proteomics workflows. An overview of the procedures for in situ proteolysis of single proteins or complex protein mixtures is reported, with a special focus on porous materials used as catalysts. The challenging efforts for designing such systems aimed at mimicking the biochemistry of living cells are reviewed. Potentials, limitations and challenges of this branch of enzyme catalysis, which we indicate as in mesopore digestion, are discussed, in relation to its suitability for high-speed and high-throughput proteomics.
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spelling pubmed-62644122018-12-10 In Mesopore Protein Digestion: A New Forthcoming Strategy in Proteomics Savino, Rocco Casadonte, Francesca Terracciano, Rosa Molecules Review The conventional protocols for in solution or in gel protein digestion require many steps and long reaction times. The use of trypsin immobilized onto solid supports has recently captured the attention of many research groups, because these systems can speed-up protein digestion significantly. The utilization of new materials such as mesoporous silica as supports, in which enzyme and substrate are dramatically concentrated and confined in the nanospace, offers new opportunities to reduce the complexity of proteomics workflows. An overview of the procedures for in situ proteolysis of single proteins or complex protein mixtures is reported, with a special focus on porous materials used as catalysts. The challenging efforts for designing such systems aimed at mimicking the biochemistry of living cells are reviewed. Potentials, limitations and challenges of this branch of enzyme catalysis, which we indicate as in mesopore digestion, are discussed, in relation to its suitability for high-speed and high-throughput proteomics. MDPI 2011-07-15 /pmc/articles/PMC6264412/ /pubmed/21765391 http://dx.doi.org/10.3390/molecules16075938 Text en © 2011 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Review
Savino, Rocco
Casadonte, Francesca
Terracciano, Rosa
In Mesopore Protein Digestion: A New Forthcoming Strategy in Proteomics
title In Mesopore Protein Digestion: A New Forthcoming Strategy in Proteomics
title_full In Mesopore Protein Digestion: A New Forthcoming Strategy in Proteomics
title_fullStr In Mesopore Protein Digestion: A New Forthcoming Strategy in Proteomics
title_full_unstemmed In Mesopore Protein Digestion: A New Forthcoming Strategy in Proteomics
title_short In Mesopore Protein Digestion: A New Forthcoming Strategy in Proteomics
title_sort in mesopore protein digestion: a new forthcoming strategy in proteomics
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6264412/
https://www.ncbi.nlm.nih.gov/pubmed/21765391
http://dx.doi.org/10.3390/molecules16075938
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