Abstract
The interaction of crystallins with lens membranes and liposomes was studied by fluorescence and circular dichroism (CD) measurements. Two extrinsic fluorescence probes ANS (1-anilino-naphthalene-8-sulfonic acid) and DPH (1,6-diphenyl, 1,3,5-hexatriene) were used to detect the binding and to explore the binding site. The ANS fluorescence intensity is greater in membranes than in liposomes, but is reverse for DPH. Among α, β and γ-crystallins, only α c-crystallin decreased the ANS fluorescence intensity in membranes, indicating a binding between membranes and α c-crystallin. The binding site appears to be at the polar-apolar interface in membrane protein (MIP26) and α c-crystallin. Fluorescence polarization measurements show that lipid bilayer becomes less mobile with α c-crystallin binding. The change in the near UV CD due to the binding also indicates a decreased freedom of rotation of aromatic amino acid residues either in MIP26 or in α-crystallin.
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