Analysis of Time-resolved Fluorescence Anisotropy in Lipid-protein Systems. I. Application to the Lipid Probe Octadecyl Rhodamine B in Interaction with Bacteriophage M13 Coat Protein Incorporated in Phospholipid Bilayers

Overview

Journal Eur Biophys J

Specialty Biophysics

Date 1990 Jan 1

PMID 2369870

Authors

K Peng

A J Visser

A van Hoek

C J Wolfs

J C Sanders

M A Hemminga

Affiliations

Soon will be listed here.

Abstract

Fluorescent probes located in heterogeneous environments give rise to anomalous time-resolved fluorescence anisotropy. A simple analytical expression of anisotropy has been derived for the case of a small difference in local fluorescence lifetimes. The expression has the diagnostic advantage that the time dependence of the fluorescence anisotropy can be predicted from the differences in fluorescence lifetimes and residual anisotropies of the probes located in different sites. Using this model, the local fluorescence anisotropy parameters and the relative contributions of the lipid probe octadecyl rhodamine B in a lipid environment and in the vicinity of bacteriophage M13 coat protein reconstituted in phospholipid bilayers, composed of 80% 1,2-dimyristoyl-sn-glycero-3-phosphocholine and 20% 1,2-dimyristoyl-sn-glycero-3-phosphoglycerol have been determined experimentally. At 40 degrees C, the correlation times for bound and free probes are 2.3 and 3.0 ns, respectively, while the corresponding order parameters are 0.85 and 0.62, respectively.

References

Kinosita Jr K, Kawato S, Ikegami A . A theory of fluorescence polarization decay in membranes. Biophys J. 1977; 20(3):289-305. PMC: 1473359. DOI: 10.1016/S0006-3495(77)85550-1. View

Datema K, Wolfs C, Marsh D, Watts A, Hemminga M . Spin-label electron spin resonance study of bacteriophage M13 coat protein incorporation into mixed lipid bilayers. Biochemistry. 1987; 26(24):7571-4. DOI: 10.1021/bi00398a006. View

van der Meer W, Pottel H, Herreman W, Ameloot M, Hendrickx H, Schroder H . Effect of orientational order on the decay of the fluorescence anisotropy in membrane suspensions. A new approximate solution of the rotational diffusion equation. Biophys J. 1984; 46(4):515-23. PMC: 1435014. DOI: 10.1016/S0006-3495(84)84049-7. View

Vos K, van Hoek A, Visser A . Application of a reference convolution method to tryptophan fluorescence in proteins. A refined description of rotational dynamics. Eur J Biochem. 1987; 165(1):55-63. DOI: 10.1111/j.1432-1033.1987.tb11193.x. View

Kinosita Jr K, Ikegami A, Kawato S . On the wobbling-in-cone analysis of fluorescence anisotropy decay. Biophys J. 1982; 37(2):461-4. PMC: 1328828. DOI: 10.1016/S0006-3495(82)84692-4. View

van Hoek A, Vervoort J, Visser A . A subnanosecond resolving spectrofluorimeter for the analysis of protein fluorescence kinetics. J Biochem Biophys Methods. 1983; 7(3):243-54. DOI: 10.1016/0165-022x(83)90033-7. View

Datema K, Visser A, van Hoek A, Wolfs C, Spruijt R, Hemminga M . Time-resolved tryptophan fluorescence anisotropy investigation of bacteriophage M13 coat protein in micelles and mixed bilayers. Biochemistry. 1987; 26(19):6145-52. DOI: 10.1021/bi00393a030. View

Heyn M . Determination of lipid order parameters and rotational correlation times from fluorescence depolarization experiments. FEBS Lett. 1979; 108(2):359-64. DOI: 10.1016/0014-5793(79)80564-5. View

Knippers R, HOFFMANN-BERLING H . A coat protein from bacteriophage fd. I. Hydrodynamic measurements and biological characterization. J Mol Biol. 1966; 21(2):281-92. DOI: 10.1016/0022-2836(66)90099-4. View

10.

van Paridon P, Shute J, Wirtz K, Visser A . A fluorescence decay study of parinaroyl-phosphatidylinositol incorporated into artificial and natural membranes. Eur Biophys J. 1988; 16(1):53-63. DOI: 10.1007/BF00255326. View

11.

Alcala J, Gratton E, Prendergast F . Fluorescence lifetime distributions in proteins. Biophys J. 1987; 51(4):597-604. PMC: 1329931. DOI: 10.1016/S0006-3495(87)83384-2. View

12.

Lipari G, Szabo A . Effect of librational motion on fluorescence depolarization and nuclear magnetic resonance relaxation in macromolecules and membranes. Biophys J. 1980; 30(3):489-506. PMC: 1328752. DOI: 10.1016/S0006-3495(80)85109-5. View

13.

Alcala J, Gratton E, Prendergast F . Interpretation of fluorescence decays in proteins using continuous lifetime distributions. Biophys J. 1987; 51(6):925-36. PMC: 1330026. DOI: 10.1016/S0006-3495(87)83420-3. View

14.

Wolber P, Hudson B . Bilayer acyl chain dynamics and lipid-protein interaction: the effect of the M13 bacteriophage coat protein on the decay of the fluorescence anisotropy of parinaric acid. Biophys J. 1982; 37(1):253-62. PMC: 1329133. DOI: 10.1016/S0006-3495(82)84674-2. View

15.

Hoekstra D, de Boer T, Klappe K, Wilschut J . Fluorescence method for measuring the kinetics of fusion between biological membranes. Biochemistry. 1984; 23(24):5675-81. DOI: 10.1021/bi00319a002. View

16.

Ludescher R, Peting L, Hudson S, Hudson B . Time-resolved fluorescence anisotropy for systems with lifetime and dynamic heterogeneity. Biophys Chem. 1987; 28(1):59-75. DOI: 10.1016/0301-4622(87)80075-3. View