What is it about?
In this work we describe the determined and refined at atomic resolution structure of the nonapeptide antibiotics helioferins A and B isolated from a natural biological source and co-crystallized with molar ratio 1:1. The peptides are expected to be positively charged as they bind fluoride and chloride anions with molar ratio 0.67:0.33. We have also compared the structure with that of the decapeptide leucinostatin A, which is the only other structure of a lipoaminopeptide known to date.
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Why is it important?
Helioferin and the earlier determined structure of the homologous leucinostatin A have total straight length of about 21 Å. This implies that their membrane-modifying antibiotic activity may not obey the pore-forming, barrel stave model. The latter model generally applies for the bioactivity of long peptaibols. In contrast, shorter lipoaminopeptide antibiotics may act via a concentration dependent aggregation in the membranes (carpet mechanism).
Perspectives
The reported structure may facilitate the interpretation of future electro-chemical experiments with artificial membranes. The latter experiments are crucial for the elucidation of the molecular function of the lipoaminopeptides.
Dr. Kyriacos Petratos
IMBB-FoRTH
Read the Original
This page is a summary of: The crystal structure of the lipoaminopeptaibol helioferin, an antibiotic peptide fromMycogone rosea, Acta Crystallographica Section D Structural Biology, April 2018, International Union of Crystallography,
DOI: 10.1107/s2059798318001857.
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