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PLoS One. 2017 Jun 27;12(6):e0179962. doi: 10.1371/journal.pone.0179962. eCollection 2017.

Structure, dynamics and kinetics of two-component Lantibiotic Lichenicidin.

Author information

1
Department of Biophysical Chemistry, Institut für Chemie, Technische Universität Berlin, Berlin, Germany.
2
Departamento de Física de la Materia Condensada, Universidad de Zaragoza, Zaragoza, Spain.
3
Instituto de Biocomputación y Física de Sistemas Complejos, Universidad de Zaragoza, Zaragoza, Spain.

Abstract

Two variants of the two-component Lantibiotic Lichenicidin, produced by the strains B. Licheniformis VK21 and I89 (Lchα/ Lchβ and Bliα/ Bliβ peptides, respectively) have been investigated by means of 2 μs-long all-atom molecular dynamics simulations combined with Markov State Models. This rigorous statistical analysis enabled to evaluate the dynamic and kinetic properties of the aforementioned systems which are not accessible via experimental techniques. The structural flexibility characteristic of these small peptides is understood by a delicate equilibrium between random coil, α-helices and β-sheet structures. The undergoing secondary structure transitions from an α-helix to a β-sheet observed for Lchα and Lchβ peptides, were not present in the Bliα component and provide new insights to understand their mechanism of action.

PMID:
28654661
PMCID:
PMC5487065
DOI:
10.1371/journal.pone.0179962
[Indexed for MEDLINE]
Free PMC Article

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