Methods for mapping protease specificity.
The study of protease specificity provides information on active-site structure and function, protein-protein interaction, regulation of intracellular and extracellular pathways, and evolution of protease and substrate genes. Peptide libraries that include fluorogenic and binding tags are often generated by solid-phase synthesis. Even larger explorations of cleavage site preferences employ positional scanning libraries or phage display. Microarrays enable presentation of individual peptides to proteases, DNA sequences for capture of peptide nucleic acid encoded peptides, or nanodroplets containing soluble peptide sequences. These new methods continue to inform the design of chemical inhibitors and the identification of substrates of proteases.
Diamond
Scott L
SL
Penn Center for Molecular Discovery, Institute for Medicine and Engineering, Department of Chemical and Biomolecular Engineering, 1024 Vagelos Research Laboratories, University of Pennsylvania, Philadelphia PA 19104, USA. sld@seas.upenn.edu
D000595:Amino Acid Sequence; D001665:Binding Sites; D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism; D005453:Fluorescence; D046228:Microarray Analysis / Q000379:methods*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D019151:Peptide Library; D010449:Peptide Mapping / Q000379:methods*; D012680:Sensitivity and Specificity; D013194:Staining and Labeling; D013379:Substrate Specificity
D010446:Peptide Fragments; D019151:Peptide Library; D010447:Peptide Hydrolases