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Interactive NMR and computer simulation studies of lanthionine-ring structures.

D E Palmer, D F Mierke, C Pattaroni

    Biopolymers
    |January 1, 1989
    PubMed
    Summary
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    Researchers are uncovering the complex structure of nisin, a natural peptide antibiotic. Understanding its unique ring structures and chemical bonds is key to its function.

    Area of Science:

    • Biochemistry
    • Structural Biology
    • Antimicrobial Peptides

    Background:

    • Nisin is a naturally occurring peptide antibiotic with a complex structure.
    • Its structure features five rings linked by lanthionine or methyllanthionine bridges.
    • Nisin also contains alpha, beta-unsaturated amino acids, contributing to its unique properties.

    Purpose of the Study:

    • To elucidate the detailed three-dimensional structure of nisin.
    • To understand the conformational properties of nisin's constrained fragments.
    • To lay the groundwork for determining the complete molecular structure of nisin.

    Main Methods:

    • High-resolution Nuclear Magnetic Resonance (NMR) spectroscopy was employed.
    • Interactive NMR and computational simulations were utilized.

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  • Molecular dynamics simulations were used to refine structural data.

    • Main Results:

    • Conformations for two model compounds of nisin's ring A were determined.
    • The conformation of a derivative of ring B was also established.
    • Structural information from NMR was refined using molecular dynamics.

    Conclusions:

    • The study provides significant progress in understanding nisin's complex structure.
    • The methods used are applicable to the remaining constrained fragments of nisin.
    • This conformational data will be crucial for an 'aufbau' approach to determine the entire nisin structure.