Thioether side chain cyclization for helical peptide formation: inhibitors of estrogen receptor–coactivator interactions
Abstract
Abstract: Cystine, lanthionine, and cystathionine containing cyclic peptides incorporating the signature nuclear receptor (NR) box (LXXLL) motif have been synthesized and the abilities of these peptides to inhibit estrogen receptor (ER)–coactivator interactions have been determined. We found that helicity of these peptides directly correlated with their bioactivity. Cystathionine proved to be a redox‐stable, isosteric replacement for the cystine disulfide. Cystathionine containing peptide 3 showed higher helical character and a lower inhibition constant (Ki, 7 n m) when compared with its cystine counterpart.
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- Authors
- Galande, A. K., Bramlett, K. S., Burris, T. P., Wittliff, J. L., & Spatola, A. F.
- Affiliations
- University of Louisville (US)
- Corresponding author
- Wittliff, J.L.
- Venue
- The Journal of Peptide Research
- Publisher
- Wiley
- Published
- 2004-03
- Volume
- 63
- Issue
- 3
- Pages
- 297-302
- ISSN
- 1397-002X (ISSN-L)
- OpenAlex
- W2076247712
- Cited by
- 69
- References
- 28
- Citations by year
- 2026: 1 · 2024: 3 · 2023: 1 · 2022: 3 · 2021: 3 · 2020: 3 · 2019: 2 · 2018: 3 · 2017: 6 · 2016: 7 · 2015: 5 · 2014: 5 · 2013: 3 · 2012: 4
- FWCI
- 1.30
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Peptide Research (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Estrogen and related hormone effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- helical peptides, estrogen receptor, coactivator binding, LXXLL motif, cystathionine, lanthionine, cyclic peptides, redox stability, peptide inhibitors
- MeSH terms
- Amino Acids, Sulfur, Binding, Competitive, Oligopeptides, Peptides, Cyclic, Receptors, Estrogen, Sulfides, Transcription Factors, Molecular Structure, Amino Acid Motifs
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