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Protease Proteomics

eagle-i ID


Resource Type

  1. Material analysis service


  1. Resource Description
    Due to their critical roles in biological pathways like hormone activation, proteasomal degradation, and apoptosis, proteases are essential for cellular function and viability. Proteases also participate in cellular homeostasis, inflammation, tissue remodeling, and coagulation and play an important roles in the pathogenicity and progression of many diseases such as viral infection or replication. Proteases comprise one of the largest protein families in organisms from E. coli to humans. Improved understanding of proteases will provide insight into biological systems and will likely provide a number of important new therapeutic targets. To properly function, proteases must preferentially cleave their target substrates in the presence of other proteins. While many factors impact protease substrate selection, one of the key aspects is the complementarity of the enzyme active site with the residues surrounding the cleaved bond in the substrate. As such, determination of the residues that comprise the preferred cleavage site of a protease provides critical information regarding substrate selection. Furthermore, determination of substrate specificity also provides a framework for the design of potent and selective inhibitors. We have used solution-phase substrate nanodroplet microarrays, in which fluorogenic substrates suspended in glycerol droplets are treated with aerosolized aqueous enzyme solutions, to provide protease substrate specificity profiles. These arrays allow high throughput characterization of the preferred residues on the P side of the substrate in a highly parallel and miniaturized format. We have studied the use of these arrays here to map the substrate specificity of 24 serine and cysteine proteases in a rapid and efficient manner. The combination of substrate mapping and compound screening provides critical information for training of Structure-Activity Relation (SAR) models.
  2. Service Provided by
    Penn Center for Molecular Discovery
  3. Website(s)
Provenance Metadata About This Resource Record
  1. workflow state
  2. contributor
    ggrant (Gregory Grant)
  3. created
  4. creator
    ggrant (Gregory Grant)
  5. modified
Copyright © 2016 by the President and Fellows of Harvard College
The eagle-i Consortium is supported by NIH Grant #5U24RR029825-02 / Copyright 2016