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Updated: Jul 19, 2026
11:09
Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
Published on: August 1, 2018
Solution structures of thiopeptide antibiotics.
Richard J Lewis1, Rachael A Hughes, Lilian Alcaraz
1AstraZeneca R&D Charnwood, Bakewell Road, Loughborough, Leicestershire, UK LE11 5RH.
Chemical Communications (Cambridge, England)
|October 13, 2006
Summary
Nuclear Magnetic Resonance (NMR) reveals the solution structure of amythiamicin D, identifying a key hydrogen bond. This study also presents the first evidence of thiopeptide self-association in solution.
Area of Science:
- Biochemistry
- Structural Biology
- Chemical Biology
Background:
- Thiopeptides are a class of natural products with complex structures and diverse biological activities.
- Understanding the solution conformation and aggregation behavior of thiopeptides is crucial for elucidating their mechanisms of action.
Purpose of the Study:
- To determine the solution conformation of the thiopeptide amythiamicin D using Nuclear Magnetic Resonance (NMR) spectroscopy.
- To investigate the potential for self-association of thiopeptides in solution.
Main Methods:
- Detailed Nuclear Magnetic Resonance (NMR) experiments were performed on amythiamicin D.
- Analysis of NMR data was used to establish the three-dimensional structure in solution.
Main Results:
- The solution conformation of amythiamicin D was established.
- A single intramolecular hydrogen bond between NH13 and O28 was identified.
- The study provides the first experimental evidence for self-association of thiopeptides in solution.
Conclusions:
- Amythiamicin D adopts a defined conformation in solution stabilized by an intramolecular hydrogen bond.
- Thiopeptides, including amythiamicin D, can self-associate in solution, suggesting this may be a general property of this class of molecules.
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