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Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
Published on: August 1, 2018
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Structural insight into hybrid peptide ε-helices.
Rajkumar Misra1, Gijo George2, Rahi M Reja1
1Department of Chemistry, Indian Institute of Science Education and Research, Dr. Homi Bhabha Road, Pune-411021, India. hn.gopi@iiserpune.ac.in.
Chemical Communications (Cambridge, England)
|January 24, 2020
Summary
This study reveals novel 11-helical structures formed by hybrid peptides. These unique peptide conformations utilize both chiral β3-amino acids and specific achiral gamma-amino acids.
Area of Science:
- Peptide chemistry and structural biology.
Background:
- Hybrid peptides incorporating unnatural amino acids offer unique structural possibilities.
- Controlling peptide secondary structures is crucial for designing novel biomaterials and therapeutics.
Purpose of the Study:
- To disclose the formation of unique epsilon-helical (11-helices) structures.
- To investigate the role of beta,gamma-hybrid peptides in forming these novel helical organizations.
Main Methods:
- Synthesis of beta,gamma-hybrid peptides containing chiral beta3-amino acids and achiral dimethyl-substituted gamma-amino acids.
- Structural analysis to confirm the formation of 11-helical conformations.
Main Results:
- Demonstration of unique epsilon-helical (11-helices) organizations.
- Successful incorporation of specific chiral beta3-amino acids and achiral gamma-amino acids to achieve these structures.
Conclusions:
- Beta,gamma-hybrid peptides can adopt unique 11-helical structures.
- This finding expands the repertoire of accessible peptide secondary structures.
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