Fluorescence quenching at interfaces and the permeation of acrylamide and iodide across phospholipid bilayers

FEBS Letters

Goñi, Félix M.¹  Moro, Fernando¹  Urbaneja, M.Angeles¹ 

[1] Department of Biochemistry, University of the Basque Country, P. O. Box 644, 48080 Bilbao, Spain

关键词: Fluorescence quenching;    Lipid bilayer;    Tryptophan;    EYPC;    egg-yolk phosphatidylcholine;    PC;    phosphatidylcholine;    12-AS;    12-(9-anthroyloxy) stearic acid;    LUV;    large unilamellar vesicles;    MLV;    multilamellar vesicles;   

DOI  :  10.1016/0014-5793(93)80257-U

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Studies of fluorescence quenching in membrane proteins are complicated by the fact that the barrier effect of the bilayer towards the quenchers is not known with precision. Our studies show that (a) both acrylamide and iodide can permeate the membrane at comparable rates, (b) when quenchers are added externally to a vesicle suspension, the apparent Stern-Volmer quenching constants for the same fluorophores are lower in the inner than in the outer aqueous compartments, and (c) at least some non-polar fluorophores embedded in the bilayer are quenched by iodide, but not by acrylamide.

【 授权许可】

Unknown