title: Melittin-induced conformational changes in human lens protein.
abstract: 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.
authors.affiliation: Division of Crystallography and Molecular Biology, Saha Institute of Nuclear Physics, Calcutta, India.
authors.forename: S K
authors.initials: SK
authors.lastname: Ghosh
authors.forename: D
authors.initials: D
authors.lastname: Chattopadhyay
authors.forename: A C
authors.initials: AC
authors.lastname: Sen
authors.forename: B
authors.initials: B
authors.lastname: Chakrabarti
mesh_terms: 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
chemical_list: D003459:Crystallins; D008555:Melitten