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LCxLCProt SIGNED

Comprehensive two-dimensional liquid chromatography for the characterization of protein biopharmaceuticals at the protein level

Total Cost €

0

EC-Contrib. €

0

Partnership

0

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Project "LCxLCProt" data sheet

The following table provides information about the project.

Coordinator
UNIVERSITEIT GENT 

Organization address
address: SINT PIETERSNIEUWSTRAAT 25
city: GENT
postcode: 9000
website: http://www.ugent.be

contact info
title: n.a.
name: n.a.
surname: n.a.
function: n.a.
email: n.a.
telephone: n.a.
fax: n.a.

 Coordinator Country Belgium [BE]
 Total cost 89˙160 €
 EC max contribution 89˙160 € (100%)
 Programme 1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility)
 Code Call H2020-MSCA-IF-2018
 Funding Scheme MSCA-IF-EF-ST
 Starting year 2020
 Duration (year-month-day) from 2020-01-01   to  2020-12-31

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    UNIVERSITEIT GENT BE (GENT) coordinator 89˙160.00

Map

 Project objective

Protein biopharmaceuticals, which globally represent about 20 % of the total pharmaceutical market, are becoming increasingly popular in the treatment of various diseases. Experts forecast that over 50 % of new drug approvals in the next decade will be for biologics, especially monoclonal antibodies. Very accurate structural characterization and purity analysis is required during both the development of the new drugs, and later during manufacturing for quality control purposes. Biopharmaceutical protein molecules are very large and heterogeneous, which makes their characterization very difficult. The goal of this project is to develop novel methods for the characterization of protein biopharmaceuticals at the protein level based on comprehensive two-dimensional liquid chromatography (LC×LC). Two approaches will be explored: the use of reversed phase separation mechanism in both dimensions with parallel gradients, and application of thermally responsive stationary phases for thermal modulation of LC×LC fractions. Parallel gradients provide the greatest orthogonality when the separation mechanisms in both dimensions are correlated, and allow the use of short modulation periods, which together lead to a dramatic increase in peak capacity (as demonstrated in preliminary experiments). Thermally responsive stationary phases allow trapping of the analyte bands at elevated temperatures, and their release at low temperature. This is compatible with intact protein analysis, especially when ion exchange is used in the first dimension of the LC×LC system. It is expected that the research will result in new, cutting edge methods for the analysis and characterization of protein biopharmaceuticals that will be applicable under the good manufacturing practice (GMP) conditions, improving the quality assurance/quality control and increasing the confidence in the pharmaceuticals.

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The information about "LCXLCPROT" are provided by the European Opendata Portal: CORDIS opendata.

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lastchecktime (2020-11-30 7:17:14) correctly updated