Resonance assignment and structural characterization of pharmacologically relevant proteins promise to improve understanding and safety of these proteins by rational design. However, the PEG coating that is used to evade the immune system also causes these molecules to "evade" the standard structural biology methodologies. We here demonstrate that it is possible to obtain the resonance assignment and a reliable structural model of large PEGylated proteins through an integrated approach encompassing NMR and X-ray crystallography.

Characterization of PEGylated Asparaginase: New Opportunities from NMR Analysis of Large PEGylated Therapeutics / Cerofolini, Linda; Giuntini, Stefano; Carlon, Azzurra; Ravera, Enrico; Calderone, Vito; Fragai, Marco; Parigi, Giacomo; Luchinat, Claudio. - In: CHEMISTRY-A EUROPEAN JOURNAL. - ISSN 0947-6539. - STAMPA. - 25:(2019), pp. 1-9. [10.1002/chem.201804488]

Characterization of PEGylated Asparaginase: New Opportunities from NMR Analysis of Large PEGylated Therapeutics

Cerofolini, Linda;Giuntini, Stefano;Carlon, Azzurra;Ravera, Enrico;Calderone, Vito;Fragai, Marco;Parigi, Giacomo;Luchinat, Claudio
2019

Abstract

Resonance assignment and structural characterization of pharmacologically relevant proteins promise to improve understanding and safety of these proteins by rational design. However, the PEG coating that is used to evade the immune system also causes these molecules to "evade" the standard structural biology methodologies. We here demonstrate that it is possible to obtain the resonance assignment and a reliable structural model of large PEGylated proteins through an integrated approach encompassing NMR and X-ray crystallography.
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Cerofolini, Linda; Giuntini, Stefano; Carlon, Azzurra; Ravera, Enrico; Calderone, Vito; Fragai, Marco; Parigi, Giacomo; Luchinat, Claudio
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/2158/1148112
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