Glycothiohexide alpha, a novel antibiotic produced by "Sebekia" sp., LL-14E605. III. Structural elucidation.

@article{Northcote1994GlycothiohexideAA,
  title={Glycothiohexide alpha, a novel antibiotic produced by "Sebekia" sp., LL-14E605. III. Structural elucidation.},
  author={Peter T Northcote and Marshall M. Siegel and Donald B. Borders and M. D. Lee},
  journal={The Journal of antibiotics},
  year={1994},
  volume={47 8},
  pages={
          901-8
        }
}
The chemical structure of a novel thiopeptide antibiotic, glycothiohexide alpha (1), isolated from the fermentation broth of a "Sebekia" species was determined based on extensive 2D NMR studies, as well as, IR, UV, and mass spectral data. The chemical structure of glycothiohexide alpha is closely related to nosiheptide (3) and antibiotic S-54832A. 
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Glycothiohexides, novel antibiotics produced by "Sebekia" sp. LL-14E605. I. Taxonomy, fermentation and biological evaluation.

The new glycothiohexide antibiotics, which are related to nosiheptide, were identified in fermentations of an actinomycete belonging to the genus "Sebekia" and failed to protect mice against a lethal challenge with Staphylococcus aureus Smith unless it was administered prior to challenge.

Potent Antibiotic Lemonomycin: A Glimpse of Its Discovery, Origin, and Chemical Synthesis

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Isolation and Structure Elucidation of Thiazomycin

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Activity of the thiopeptide antibiotic nosiheptide against contemporary strains of methicillin-resistant Staphylococcus aureus

Nosiheptide represents a promising antibiotic for the treatment of serious infections caused by contemporary strains of MRSA and exhibited a significantly prolonged post-antibiotic effect against both healthcare- and community-associated MRSA compared with vancomycin.

Importance of Noncovalent Interactions Involving Sulfur Atoms in Thiopeptide Antibiotics─Glycothiohexide α and Nocathiacin I.

The roles of sulfur-based noncovalent interactions in complex naturally occurring molecules representative of thiopeptide antibiotics: glycothiohexide α and its close structural analogue nocathiacin I are examined.

Occurrence, distribution, dereplication and efficient discovery of thiazolyl peptides by sensitive-resistant pair screening

A highly effective library-based dereplication of thiazolyl peptides by high resolution fourier transform liquid chromatography mass spectrometry (HRFTLCMS) has been developed, which can detect and dereplicate very low levels of thIAe peptides particularly when combined with miniaturized high-throughput 96-well solid-phase extraction separation, and as well can be automated.

Natural thiopeptides as a privileged scaffold for drug discovery and therapeutic development

The thiazolyl peptides (thiopeptides), an ever-expanding family of antibiotics produced by Gram-positive bacteria that have attracted the interest of many research groups thanks to their novel chemical structures and outstanding biological profiles, are reviewed.

YcaO-Dependent Posttranslational Amide Activation: Biosynthesis, Structure, and Function.

The formerly enigmatic YcaO superfamily (DUF181), has been found to catalyze a unique phosphorylation of a ribosomal peptide backbone amide upon attack by different nucleophiles.