FT-RAMAN STUDIES ON THE TRANSFORMATION OF G-ACTIN TO F-ACTIN, THE BINDING OF CISPLATIN AND TRANSPLATIN TO F-ACTIN AND THE EFFECTS OF THE CONFORMATION OF F-ACTIN
Hh. Zeng et al., FT-RAMAN STUDIES ON THE TRANSFORMATION OF G-ACTIN TO F-ACTIN, THE BINDING OF CISPLATIN AND TRANSPLATIN TO F-ACTIN AND THE EFFECTS OF THE CONFORMATION OF F-ACTIN, International journal of biological macromolecules, 20(2), 1997, pp. 107-113
The conformation change of G-actin to F-actin and the binding modes of
cisplatin and transplatin to F-actin have been studied by FT-Raman sp
ectroscopy. The studies show that the process of polymerization is rel
ated to the vibration of C-S Gauche mode (similar to 650 cm(-1)), whic
h indicates that the methionine (Met) contributes to the polymerizatio
n of actin. The relative intensity of I(925)/I(803), reflecting the co
nformation of actin secondary structure, does not change during the po
lymerization process. The effect of cisplatin and transplatin on F-act
in is dependent on the species and their concentrations. Cisplatin, at
high concentrations, affects the conformation of F-actin mainly by bi
nding with the sulphur of methionine. Transplatin, even at low concent
rations, obviously affects the F-actin's conformation due to it's mult
iple binding sites, on N-containing sites in addition to S-methionine
sites. These results relate to the differences in pharmacology and tox
icology effects of the complexes. (C) 1997 Elsevier Science B.V.