Chemical modification of thiol group(s) in protein: application to the study of anti-microtubular drugs binding.
1. Different chemical procedures such as performic oxidation, carboxymethylation, carboxyethylation, aminoethylation, cyanylation, acylation, arylation etc. and addition of thiols to activated double bonds, titration of thiols with DTNB (Dithiobis-Nitro-Benzoate) and the reaction of thiols with organomercurials and the titration with p-chloro-mercuri-benzoate (PCMB) etc. are cited and discussed. Their chemical reactions are shown in the figures. 2. We describe in this paper that several chemicals interfere with microtubule assembly by combining with sulfhydryl residues. Reagents such as Cytochalasin-A and B, ethylacetylacrylate, FDNB (fluorodinitrobenzene), NEM (N-ethyl-maleimide), diamide, EBI (ethylene-bis-iodoacetamide, ethacrynic acid, methal ions, methylmercury, triethyllead ion and CDDP (cis-dichlorodiammine-platinum-II) are cited and their mechanisms are discussed.
Han
K K
KK
Laboratoire des Neurosciences, Unité INSERM No. 16, Lille, France.
Delacourte
A
A
Hemon
B
B
D001665:Binding Sites; D055598:Chemical Phenomena; D002621:Chemistry; D008870:Microtubules / Q000187:drug effects*; D011506:Proteins; D013438:Sulfhydryl Compounds; D013439:Sulfhydryl Reagents / Q000494:pharmacology; D014404:Tubulin
D011506:Proteins; D013438:Sulfhydryl Compounds; D013439:Sulfhydryl Reagents; D014404:Tubulin