title: Enzyme-triggered gelation: targeting proteases with internal cleavage sites.
abstract: A generalizable method for detecting protease activity via gelation is described. A recognition sequence is used to target the protease of interest while a second protease is used to remove the residual residues from the gelator scaffold. Using this approach, selective assays for both MMP-9 and PSA are demonstrated.
authors.affiliation: Department of Chemistry and Macromolecular Science and Engineering Program, University of Michigan, 930 North University Avenue, Ann Arbor, Michigan, 48109-1055, USA. ajmcneil@umich.edu.
authors.forename: Steven C
authors.initials: SC
authors.lastname: Bremmer
authors.forename: Anne J
authors.initials: AJ
authors.lastname: McNeil
authors.forename: Matthew B
authors.initials: MB
authors.lastname: Soellner
mesh_terms: D001665:Binding Sites; D015374:Biosensing Techniques; D018826:CD13 Antigens / Q000378:metabolism; D057075:Enzyme Assays / Q000379:methods*; D005782:Gels; D020780:Matrix Metalloproteinase 9 / Q000378:metabolism*; D017430:Prostate-Specific Antigen / Q000378:metabolism*
chemical_list: D005782:Gels; D018826:CD13 Antigens; D017430:Prostate-Specific Antigen; D020780:Matrix Metalloproteinase 9