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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.

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Apr 8th, 12:00 AM Apr 8th, 12:00 AM

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