Synthesis, Characterization, and DNA Binding Profile of a Macrocyclic β‑Sheet Analogue of ARC Protein

July 28, 2017

Title

Synthesis, Characterization, and DNA Binding Profile of a Macrocyclic β‑Sheet Analogue of ARC Protein

Author

Azzurra Stefanucci, Jesús Mosquera, Eugènio Vázquez, José L. Mascareñas, Ettore Novellino, Adriano Mollica

Year

2015

Journal

ACS Medicinal Chemistry Letters

Abstract

ARC repressor (apoptosis repressor with caspase recruitment domain) is a protein which binds selectively to a specific sequence of DNA. In humans, ARC is primarily expressed in striated muscle tissue, which normally does not undergo rapid cell turnover. This suggests that ARC may play a protective role in the prevention against Duchenne Muscular Dystrophy and several types of tumors. In this Letter we report the synthesis, characterization, and conformational analysis of a β-sheet ARC repressor mimetic, based on the amino acid sequence of the β-sheet domain in the ARC protein. The ability of this β-sheet macrocycle to bind to double-stranded DNA was also evaluated using spectroscopic methods. Our data show that the synthetic peptide has a defined conformation and is able to bind DNA with reasonable affinity. These initial results lay the groundwork for the design of novel β-sheets folded peptides as valuable substitutes of transcription factor proteins in drug therapy.

Instrument

J-715

Keywords

Circular dichroism, Protein folding, Ligand binding, Biochemistry, Medicinal