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G Dietler

Publications and source records attributed to G Dietler.

25 records · Page 2Linked to original sources
PubMed1985

Temperature dependence of fibrin polymerization: a light scattering study.

The aggregation of fibrin occurring in a fibrinogen solution upon addition of the enzyme thrombin has been studied prior to the sol-gel transition at different temperatures by means of dynamic light scattering and simultaneous measurement of the released fibrinopeptide A (FPA). The evolution of the polymer distribution with time was found to be independent of the temperature. The analysis of the experiments yields the explanation: with increasing temperature the rate of FPA release increases because it involves an activation energy, whereas the aggregation rate of the fibrin monomers decreases because it is exothermic. The light scattering experiments show that the state of aggregation is a chemical equilibrium that can be shifted by the addition of the tetrapeptide Gly-Pro-Arg-Pro. From dynamic light scattering data it is possible to derive the probability of bond formation between fibrin molecules and from it the aggregation enthalpy. For 30 degrees C a value of -19 kcal/mol was obtained.

Fibrin↗
PubMed1982

Fibrin aggregation before sol-gel transition.

Fibrinogen solutions (concentrations 2 mg/ml, 0.15-M Tris-NaCl buffer, pH 7.4) were incubated at 20 degrees C with quantities of reptilase or thrombin that were so small that the polymerization process could be followed for several hours by means of static and dynamic light scattering. The scattered intensity and its correlation function were recorded at scattering angles between 30 degrees and 150 degrees. The measured data were compared with model calculations based on the Flory-Stockmayer distribution, which predicts a sol-gel phase transition. This distribution is characterized by a parameter, lambda, that indicates the extent of aggregation. lambda = 0 corresponds to the monomeric solution, and lambda = 1 indicates the sol-gel transition. Good agreement was found for monomeric units of 75-nm length aggregating (a) end-to-end in the early stage (0 less than or equal to lambda less than or equal to 0.3), and (b) in a staggered overlap pattern for the progressing polymerization (0.3 less than or equal to lambda less than 1). Before the gel point was reached, no systemic difference was observed between the data obtained after activation with thrombin which releases both fibrinopeptides A and B from fibrinogen, and reptilase, which exclusively releases the fibrinopeptides A. This confirms that the release of the fibrinopeptides A is the essential prerequisite for the aggregation process.

Batroxobin↗
PubMedDate not supplied

Near-field optical excitation as a dipole-dipole energy transfer process.

The process of fluorescence excitation in the scanning near-field optical microscope (SNOM) is considered as a dipole-dipole resonance energy transfer process between a molecule under study and a SNOM aperture, which can be treated as a magnetic-type point dipole. It is shown that such an approach satisfactorily describes the conditions of the usual SNOM fluorescence experiments. Fluorescence excitation dependence on the polarization of the incident light and medium refraction index have been obtained. The equation to calculate the resonance dipole-dipole energy transfer radius (which is a natural unit of a SNOM's longitudinal resolution) is derived. Those cases where such a radius is of the order of the SNOM aperture, and thus single dipole, can strongly influence the radiation conditions are discussed briefly.

Journal Article↗