title: Using peptidyl aldehydes in activity-based proteomics.
abstract: The broad inhibitory spectrum of aldehydes and the possibility that amino acid residues modulate their specificity point to the potential of using peptidyl aldehydes as activity-based probes. Here, we establish the potential of peptidyl aldehydes in activity-based proteomics by synthesizing different probes and using them to specifically label a well-known serine protease in an activity-dependent manner. From our results, peptidyl aldehydes emerge as promising activity-based probes that enable multiple enzymatic-class detection by substrate recognition and can be used in diverse activity-based proteomics applications like protein identification and activity profiling.
authors.affiliation: Universitat de Barcelona, Departament de Química Orgànica, Barcelona, Spain.
authors.forename: Eduard
authors.initials: E
authors.lastname: Sabidó
authors.forename: Teresa
authors.initials: T
authors.lastname: Tarragó
authors.forename: Ernest
authors.initials: E
authors.lastname: Giralt
mesh_terms: D000447:Aldehydes / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology; D000595:Amino Acid Sequence; D000818:Animals; D020134:Catalytic Domain; D051379:Mice; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology; D000085822:Prolyl Oligopeptidases; D040901:Proteomics; D012697:Serine Endopeptidases / Q000737:chemistry / Q000378:metabolism; D015842:Serine Proteinase Inhibitors / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology
chemical_list: D000447:Aldehydes; D010455:Peptides; D015842:Serine Proteinase Inhibitors; D012697:Serine Endopeptidases; D000085822:Prolyl Oligopeptidases