Melittin-induced conformational changes in human lens protein.
Circular dichroism and fluorescence measurements showed a reduced conformational order in proteins of a normal human lens when they were incubated in vitro with melittin, a bee venom peptide. Since melittin is also known to react with lipids to induce a breakdown of vesicular structure, the observed denaturation of water-soluble proteins of a human lens that developed a cataract due to multiple bee stings may be accounted for by the effects of melittin to some extent. The melittin-induced decrease of conformational order, as observed in our in-vitro studies could thus be of physiological significance.
Ghosh
S K
SK
Division of Crystallography and Molecular Biology, Saha Institute of Nuclear Physics, Calcutta, India.
Chattopadhyay
D
D
Sen
A C
AC
Chakrabarti
B
B
D002942:Circular Dichroism; D003459:Crystallins / Q000737:chemistry*; D006801:Humans; D007908:Lens, Crystalline / Q000737:chemistry*; D008555:Melitten / Q000737:chemistry*; D008875:Middle Aged; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence
D003459:Crystallins; D008555:Melitten