title: Current and prospective applications of non-proteinogenic amino acids in profiling of proteases substrate specificity.
abstract: Proteases recognize their endogenous substrates based largely on a sequence of proteinogenic amino acids that surrounds the cleavage site. Currently, several methods are available to determine protease substrate specificity based on approaches employing proteinogenic amino acids. The knowledge about the specificity of proteases can be significantly extended by application of structurally diverse families of non-proteinogenic amino acids. From a chemical point of view, this information may be used to design specific substrates, inhibitors, or activity-based probes, while biological functions of proteases, such as posttranslational modifications can also be investigated. In this review, we discuss current and prospective technologies for application of non-proteinogenic amino acids in protease substrate specificity profiling.
authors.affiliation: Division of Bioorganic Chemistry, Faculty of Chemistry, Wroclaw University of Technology, 50-370 Wroclaw, Poland.
authors.forename: Paulina
authors.initials: P
authors.lastname: Kasperkiewicz
authors.forename: Anna D
authors.initials: AD
authors.lastname: Gajda
authors.forename: Marcin
authors.initials: M
authors.lastname: Drąg
mesh_terms: D000596:Amino Acids / Q000737:chemistry / Q000378:metabolism*; D010450:Endopeptidases / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D010447:Peptide Hydrolases / Q000737:chemistry / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D000596:Amino Acids; D010450:Endopeptidases; D010447:Peptide Hydrolases