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Faculty Sponsor
Dr. Bryan Knuckley PhD
Faculty Sponsor College
College of Arts and Sciences
Faculty Sponsor Department
Chemistry
Location
SOARS Virtual Conference
Presentation Website
https://unfsoars.domains.unf.edu/identification-of-histone-h4-based-peptoids-as-inhibitors-of-prmt1/
Keywords
SOARS (Conference) (2020 : University of North Florida) -- Posters; University of North Florida. Office of Undergraduate Research; University of North Florida. Graduate School; College students – Research -- Florida – Jacksonville -- Posters; University of North Florida – Undergraduates -- Research -- Posters; University of North Florida. Department of Chemistry -- Research -- Posters; Biology; Physics; and Chemistry -- Research – Posters
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.
Included in
Identification of Histone H4-Based Peptoids as Inhibitors of PRMT1
SOARS Virtual Conference
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.
https://digitalcommons.unf.edu/soars/2020/spring_2020/19