Sordarin sodium

Modify Date: 2024-01-11 16:21:47

Sordarin sodium Structure
Sordarin sodium structure
Common Name Sordarin sodium
CAS Number 463356-00-5 Molecular Weight 514.58
Density N/A Boiling Point N/A
Molecular Formula C27H39NaO8 Melting Point N/A
MSDS USA Flash Point N/A

 Use of Sordarin sodium


Sordarin is a potent diphthamide-dependent eEF2 inhibitor with antifungal properties. Sordarin targets eEF2 so as to inhibit protein translation by blocking eEF2-mediated translocation of tRNAs. Sordarin inhibits translation specifically in certain fungi (e.g. C. albicans, C. glabrata, and C. neoformans) while unable to do so in some other fungal species (e.g. Candida parapsilosis and Candida lusitaniae)[1][2].

 Names

Name Sordarin sodium

 Sordarin sodium Biological Activity

Description Sordarin is a potent diphthamide-dependent eEF2 inhibitor with antifungal properties. Sordarin targets eEF2 so as to inhibit protein translation by blocking eEF2-mediated translocation of tRNAs. Sordarin inhibits translation specifically in certain fungi (e.g. C. albicans, C. glabrata, and C. neoformans) while unable to do so in some other fungal species (e.g. Candida parapsilosis and Candida lusitaniae)[1][2].
Related Catalog
Target

IC50: eEF2; fungal[1]

References

[1]. Wael Abdel-Fattah, et al. Insights into diphthamide, key diphtheria toxin effector. Toxins (Basel). 2013 May 3;5(5):958-68.

[2]. Biprashekhar Chakraborty, et al. Structure-based designing of sordarin derivative as potential fungicide with pan-fungal activity. J Mol Graph Model. 2016 May;66:133-42.

 Chemical & Physical Properties

Molecular Formula C27H39NaO8
Molecular Weight 514.58

 Safety Information

Personal Protective Equipment Eyeshields;Gloves;type N95 (US);type P1 (EN143) respirator filter
Hazard Codes Xi
RIDADR NONH for all modes of transport

 Articles1

More Articles
Insights into diphthamide, key diphtheria toxin effector.

Toxins (Basel.) 5(5) , 958-68, (2013)

Diphtheria toxin (DT) inhibits eukaryotic translation elongation factor 2 (eEF2) by ADP-ribosylation in a fashion that requires diphthamide, a modified histidine residue on eEF2. In budding yeast, dip...

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