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Use of monolithic supports for high-throughput protein and peptide separation in proteomics

Authorized Users Only
2017
Authors
Anđelković, Uroš
Tufegdžić, Srđan
Popović, Milica M.
Article (Published version)
Metadata
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Abstract
The exclusive properties of monolithic supports enable fast mass transfer, high porosity, low back pressure, easy preparation process and miniaturisation, and the availability of different chemistries make them particularly suitable materials for high-throughput (HTP) protein and peptide separation. In this review recent advances in monolith-based chromatographic supports for HTP screening of protein and peptide samples are presented and their application in HTP sample preparation (separation, enrichment, depletion, proteolytic digestion) for HTP proteomics is discussed. Development and applications of different monolithic capillary columns in HTP MS-based bottom-up and top-down proteomics are overviewed. By discussing the chromatographic conditions and the mass spectrometric data acquisition conditions an attempt is made to present currently demonstrated capacities of monolithic capillary columns for HTP identification and quantification of proteins and peptides from complex biologica...l samples by MS-based proteomics. Some recent advances in basic monolith technology of importance for proteomics are also discussed.

Keywords:
High-throughput / Liquid chromatography / Mass spectrometry / Monoliths / Proteomics
Source:
Electrophoresis, 2017, 38, 22-23, 2851-2869
Publisher:
  • Wiley, Hoboken
Funding / projects:
  • Production, purification and characterization of enzymes and small molecules and their application as soluble or immobilized in food biotechnology, biofuels production and environmental protection (RS-172048)
  • Interactions of natural products, their derivatives and coordination compounds with proteins and nucleic acids (RS-172055)
  • Allergens, antibodies, enzymes and small physiologically important molecules: design, structure, function and relevance (RS-172049)
  • HTP-GLYCOMET - Methods for high-throughput glycoproteomic analysis (EU-324400)
Note:
  • Peer-reviewed manuscript: http://cherry.chem.bg.ac.rs/handle/123456789/2976

DOI: 10.1002/elps.201700221

ISSN: 0173-0835

PubMed: 28906564

WoS: 000416867300006

Scopus: 2-s2.0-85029455881
[ Google Scholar ]
12
17
URI
https://cherry.chem.bg.ac.rs/handle/123456789/2557
Collections
  • Publikacije
Institution/Community
Hemijski fakultet
TY  - JOUR
AU  - Anđelković, Uroš
AU  - Tufegdžić, Srđan
AU  - Popović, Milica M.
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2557
AB  - The exclusive properties of monolithic supports enable fast mass transfer, high porosity, low back pressure, easy preparation process and miniaturisation, and the availability of different chemistries make them particularly suitable materials for high-throughput (HTP) protein and peptide separation. In this review recent advances in monolith-based chromatographic supports for HTP screening of protein and peptide samples are presented and their application in HTP sample preparation (separation, enrichment, depletion, proteolytic digestion) for HTP proteomics is discussed. Development and applications of different monolithic capillary columns in HTP MS-based bottom-up and top-down proteomics are overviewed. By discussing the chromatographic conditions and the mass spectrometric data acquisition conditions an attempt is made to present currently demonstrated capacities of monolithic capillary columns for HTP identification and quantification of proteins and peptides from complex biological samples by MS-based proteomics. Some recent advances in basic monolith technology of importance for proteomics are also discussed.
PB  - Wiley, Hoboken
T2  - Electrophoresis
T1  - Use of monolithic supports for high-throughput protein and peptide separation in proteomics
VL  - 38
IS  - 22-23
SP  - 2851
EP  - 2869
DO  - 10.1002/elps.201700221
UR  - Kon_3373
ER  - 
@article{
author = "Anđelković, Uroš and Tufegdžić, Srđan and Popović, Milica M.",
year = "2017",
abstract = "The exclusive properties of monolithic supports enable fast mass transfer, high porosity, low back pressure, easy preparation process and miniaturisation, and the availability of different chemistries make them particularly suitable materials for high-throughput (HTP) protein and peptide separation. In this review recent advances in monolith-based chromatographic supports for HTP screening of protein and peptide samples are presented and their application in HTP sample preparation (separation, enrichment, depletion, proteolytic digestion) for HTP proteomics is discussed. Development and applications of different monolithic capillary columns in HTP MS-based bottom-up and top-down proteomics are overviewed. By discussing the chromatographic conditions and the mass spectrometric data acquisition conditions an attempt is made to present currently demonstrated capacities of monolithic capillary columns for HTP identification and quantification of proteins and peptides from complex biological samples by MS-based proteomics. Some recent advances in basic monolith technology of importance for proteomics are also discussed.",
publisher = "Wiley, Hoboken",
journal = "Electrophoresis",
title = "Use of monolithic supports for high-throughput protein and peptide separation in proteomics",
volume = "38",
number = "22-23",
pages = "2851-2869",
doi = "10.1002/elps.201700221",
url = "Kon_3373"
}
Anđelković, U., Tufegdžić, S.,& Popović, M. M.. (2017). Use of monolithic supports for high-throughput protein and peptide separation in proteomics. in Electrophoresis
Wiley, Hoboken., 38(22-23), 2851-2869.
https://doi.org/10.1002/elps.201700221
Kon_3373
Anđelković U, Tufegdžić S, Popović MM. Use of monolithic supports for high-throughput protein and peptide separation in proteomics. in Electrophoresis. 2017;38(22-23):2851-2869.
doi:10.1002/elps.201700221
Kon_3373 .
Anđelković, Uroš, Tufegdžić, Srđan, Popović, Milica M., "Use of monolithic supports for high-throughput protein and peptide separation in proteomics" in Electrophoresis, 38, no. 22-23 (2017):2851-2869,
https://doi.org/10.1002/elps.201700221 .,
Kon_3373 .

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