Identification of Histone H4-Based Peptoids as Inhibitors of PRMT1

Identification of Histone H4-Based Peptoids as Inhibitors of PRMT1 poster

Audio Presentation:

 

STAFF PICK

Research Authorship:

Megan DeMart, Molly Dubose, Sarah Mann, Corey Causey, PhD, and Bryan Knuckley, PhD

Faculty Mentor:

Dr. Bryan Knuckley | College of Arts and Sciences | Department of Chemistry

Abstract:

Protein Arginine Methyltransferases (PRMTs) are a family of 11 mammalian enzymes characterized by the post-translational methylation of arginine residues in the histone tail. The majority of the 11 members of the PRMT family are divided into two main types, Type I and Type II. PRMT1, the major Type I isozyme, catalyzes the formation of asymmetrically dimethylated arginine (ADMA). PRMT1 activates transcription of cancer genes. Peptoids, or poly-N-substituted glycine’s are a class of oligomers whose side chains are appended to the nitrogen atom of the peptide backbone rather than the alpha carbon. Kinetic parameters were conducted for both peptide and peptoid sequences. The Kcat/Km and IC50 values determined that peptoids show inhibition activity. The specificity and location of these interactions are currently being determined by altering the residues of a known peptoid sequence that has these interactions.

1 thought on “Identification of Histone H4-Based Peptoids as Inhibitors of PRMT1”

  1. Karen Cousins

    This is very nicely-presented faculty-mentored research. I appreciate the addition of an audio presentation, which personalizes the project and is helpful to the non-specialist.

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