Theoretical assessment of indistinguishable peptides in mass spectrometry-based proteomics

Mass-spectrometry-based proteomics has advanced with the integration of experimental and predicted spectral libraries, which have significantly improved peptide identification in complex search spaces. However, challenges persist in distinguishing some peptides with close retention times and nearly...

Descripción completa

Detalles Bibliográficos
Autores: Elhamraoui, Zahra, Borràs, Eva, Wilhelm, Mathias, Sabidó Aguadé, Eduard, 1981-
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2024
País:España
Institución:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositorio:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:10230/68925
Acceso en línea:http://hdl.handle.net/10230/68925
http://dx.doi.org/10.1021/acs.analchem.4c02803
Access Level:acceso abierto
Palabra clave:Fragmentation
Monomers
Peptide identification
Peptides and proteins
Precursors
Descripción
Sumario:Mass-spectrometry-based proteomics has advanced with the integration of experimental and predicted spectral libraries, which have significantly improved peptide identification in complex search spaces. However, challenges persist in distinguishing some peptides with close retention times and nearly identical fragmentation patterns. In this study, we conducted a theoretical assessment to quantify the prevalence of indistinguishable peptides within the human canonical proteome and immunopeptidome using state-of-the-art retention time and spectrum prediction models. By quantifying the proportion of peptides posing challenges to unequivocal identification, we set the theoretical nonaccessible portion within a given proteome, and underscore the effectiveness of contemporary analytical methodologies in resolving the complexity of the human proteome and immunopeptidome via mass spectrometry.