Effects of Fullerene Derivatives on Activity of Ca2+-ATPase of the Sarcoplasmic Reticulum and cGMP Phosphodiesterase

L. V. Tat’yanenko, E. A. Khakina, A. V. Zhilenkov, P. A. Troshin, O. V. Dobrokhotova, I. Yu Pikhteleva, A. I. Kotel’nikov

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)


We studied the effects of new water-soluble polysubstituted fullerene C60 (PFD) derivatives on activity of Ca2+-Mg2+ ATPase of the sarcoplasmic reticulum and cGMP phosphodiesterase. All examined fullerene derivatives inhibited activity of both enzymes. For instance, PFD-I, PFD-II, PFD-III, PFD-V, PFD-IX, PFD-X, and PFD-XI in a concentration of 5×10—5 M completely inhibited hydrolytic and transport functions of Ca2+-ATPase. These compounds in a concentration of 5×10—6 suppressed active transport of calcium ions by 51±5, 77±8, 52±5, 52±5, 100±10, 80±8, and 100±10%, respectively, and inhibited ATP hydrolysis by 31±3, 78±8, 18±2, 29±3, 78±8, 63±7, and 73±9%, respectively, uncoupling the hydrolytic and transport functions of the enzyme. PFD-I noncompetitive and reversibly reduced activity of Ca2+-ATPase (Ki=2.3×10—6 M). All the studied fullerene derivatives (except for PFD-VII) inhibited cGMP phosphodiesterase by more than 80% in concentration of 10—4 M and higher and by more than 50% in concentration of 10—5 M. PFD-I is a non-competitive reversible inhibitor of cGMP phosphodiesterase (Ki=7×10—6 M). These results allow us to expect antimetastatic, antiaggregatory, antihypertensive and vasodilative activity of the studied compounds.

Original languageEnglish
Pages (from-to)321-325
Number of pages5
JournalBulletin of Experimental Biology and Medicine
Issue number3
Publication statusPublished - 1 Jul 2017
Externally publishedYes


  • Ca-Mg-ATPase of the sarcoplasmic reticulum
  • cGMP phosphodiesterase
  • fullerene derivatives
  • inhibition


Dive into the research topics of 'Effects of Fullerene Derivatives on Activity of Ca2+-ATPase of the Sarcoplasmic Reticulum and cGMP Phosphodiesterase'. Together they form a unique fingerprint.

Cite this