PUBLICATION

A highly soluble, non-phototoxic, non-fluorescent blebbistatin derivative

Authors
Várkuti, B.H., Képiró, M., Horváth, I.Á., Végner, L., Ráti, S., Zsigmond, Á., Hegyi, G., Lenkei, Z., Varga, M., Málnási-Csizmadia, A.
ID
ZDB-PUB-160601-8
Date
2016
Source
Scientific Reports   6: 26141 (Journal)
Registered Authors
Varga, Máté, Zsigmond, Aron
Keywords
Cellular imaging, Chemical modification, Myosin, Small molecules
MeSH Terms
  • Animals
  • Cell Survival/drug effects
  • Chemical Precipitation
  • Dermatitis, Phototoxic*
  • Drug Stability
  • Fluorescence*
  • HeLa Cells
  • Heterocyclic Compounds, 4 or More Rings/chemical synthesis
  • Heterocyclic Compounds, 4 or More Rings/chemistry*
  • Heterocyclic Compounds, 4 or More Rings/pharmacology
  • Heterocyclic Compounds, 4 or More Rings/toxicity*
  • Humans
  • Myosin Type II/antagonists & inhibitors
  • Rabbits
  • Solubility
  • Survival Analysis
  • Zebrafish
PubMed
27241904 Full text @ Sci. Rep.
Abstract
Blebbistatin is a commonly used molecular tool for the specific inhibition of various myosin II isoforms both in vitro and in vivo. Despite its popularity, the use of blebbistatin is hindered by its poor water-solubility (below 10 micromolar in aqueous buffer) and blue-light sensitivity, resulting in the photoconversion of the molecule, causing severe cellular phototoxicity in addition to its cytotoxicity. Furthermore, blebbistatin forms insoluble aggregates in water-based media above 10 micromolar with extremely high fluorescence and also high adherence to different types of surfaces, which biases its experimental usage. Here, we report a highly soluble (440 micromolar in aqueous buffer), non-fluorescent and photostable C15 amino-substituted derivative of blebbistatin, called para-aminoblebbistatin. Importantly, it is neither photo- nor cytotoxic, as demonstrated on HeLa cells and zebrafish embryos. Additionally, para-aminoblebbistatin bears similar myosin II inhibitory properties to blebbistatin or para-nitroblebbistatin (not to be confused with the C7 substituted nitroblebbistatin), tested on rabbit skeletal muscle myosin S1 and on M2 and HeLa cells. Due to its drastically improved solubility and photochemical feature, as well as lack of photo- or cytotoxicity, para-aminoblebbistatin may become a feasible replacement for blebbistatin, especially at applications when high concentrations of the inhibitor or blue light irradiation is required.
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Human Disease / Model
Sequence Targeting Reagents
Fish
Antibodies
Orthology
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Mapping