Ligand screening by exoproteolysis and mass spectrometry in combination with computer modelling

Josep Villanueva, Gregorio Fernández-Ballester, Enrique Querol, Francesc X. Aviles, Luis Serrano

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Resum

Here, we present a new approach for protein ligand screening based on the use of limited exoproteolysis coupled to MALDI-TOF mass spectrometry, combined with computational modelling and prediction of binding energies. As a test for this combined approach, we have screened a combinatorial library containing 8000 peptides (organized in 60 peptide samples) based on positional scanning format. This library is attached to a poly-Pro framework, and screened against the Abl-SH3 domain. The results obtained demonstrated the validity of the experimental and theoretical approaches in identifying better ligands and in rationalizing the changes in affinity. Exoproteolysis coupled to MALDI-TOF mass spectrometry could be used to screen complex libraries in a fast and efficient way. © 2003 Elsevier Ltd. All rights reserved.
Idioma originalEnglish
Pàgines (de-a)1039-1048
RevistaJournal of Molecular Biology
Volum330
Número5
DOIs
Estat de la publicacióPublicada - 25 de jul. 2003

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