Biochimica et Biophysica Acta 2015-01-01

Modulation of the mitochondrial voltage dependent anion channel (VDAC) by curcumin.

Debanjan Tewari, Tofayel Ahmed, Venkat R Chirasani, Pradeep K Singh, Samir K Maji, Sanjib Senapati, Amal Kanti Bera

Index: Biochim. Biophys. Acta 1848(1 Pt A) , 151-8, (2015)

Full Text: HTML

Abstract

Voltage dependent anion channel (VDAC) of mitochondria plays a crucial role in apoptosis. Human VDAC-1, reconstituted in planar lipid bilayer showed reduced conductance when treated with curcumin. Curcumin interacts with residues in the α helical N-terminus of VDAC and in the channel wall, as revealed by molecular docking, followed by mutational analysis. N-terminus mimicking peptide showed conformational changes in circular dichroism, upon curcumin treatment. We propose that the interaction of curcumin with amino acids in N-terminus and in channel wall fixes the α helix in closed conformation. This restricts its movement which is required for the opening of the channel. Copyright © 2014 Elsevier B.V. All rights reserved.

Related Compounds

Structure Name/CAS No. Articles
Curcumin Structure Curcumin
CAS:458-37-7
Hydroxylapatite Structure Hydroxylapatite
CAS:1306-06-5
Calcium hydroxycalcium(1+) phosphate (4:1:3) Structure Calcium hydroxycalcium(1+) phosphate (4:1:3)
CAS:12167-74-7
N-Dodecyl-N,N-dimethylamine oxide Structure N-Dodecyl-N,N-dimethylamine oxide
CAS:1643-20-5
Galanin (1-13)-Substance P (5-11) amide Structure Galanin (1-13)-Substance P (5-11) amide
CAS:138579-66-5