ArticleACS medicinal chemistry letters2015
Synthesis, Characterization, and DNA Binding Profile of a Macrocyclic β-Sheet Analogue of ARC Protein.
Article in ACS medicinal chemistry letters, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 20 citations in OpenAlex.
- Greening the Solid-Phase Peptide Synthesis of the First Bicyclic Analogue of the Arc Repressor and Its Binding to DNA.The Journal of organic chemistry · 2025Article
- Molecular Aggregation Strategy for Inhibiting DNases.JACS Au · 2024Article
- New Teixobactin Analogues with a Total Lactam Ring.ACS medicinal chemistry letters · 2023Article
- DNA major versus minor groove occupancy of monomeric and dimeric crystal violet derivatives. Toward structural correlations.Bioorganic & medicinal chemistry · 2023Article
- Peptides Mimicking the β7/β8 Loop of HIV-1 Reverse Transcriptase p51 as "Hotspot-Targeted" Dimerization Inhibitors.ACS medicinal chemistry letters · 2020Article
- On resin click-chemistry-mediated synthesis of novel enkephalin analogues with potent anti-nociceptive activity.Scientific reports · 2019Article
Corrections and comments
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Authors and funding
6 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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.
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