PubMed · 5071509
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J M Gamble, J C Peake. 1972. Electron dosimetry.. https://doi.org/10.1088/0031-9155%2F17%2F1%2F013
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PURPOSE: In breast radiotherapy, delivery of manually-calculated electron boosts limits retrospective dose-response analyses as dose distribution is unavailable. This work evaluates the feasibility of reconstructing dose distributions from manually planned electron boosts in breast-conserving radiotherapy. METHODS: Only 72 out of 198 breast cancer patients had complete stored dose distributions from sequential electron boosts in the REQUITE study. Arbitrary data from 70/72 patients were used to develop and validate dose reconstruction method. Twenty patients were used to determine optimal parameters for Monte-Carlo-based (MC) electron dose reconstruction on RayStation (v.11B-R), considering CT-calibration curve, MC-history number, andcalculation grid resolution. Remaining 50 patients were used to quantify dose reconstruction accuracy. The similarity between reconstructed and stored dose was evaluated using 3D-gamma index and dosimetric parameters extracted from breast and tumour bed contours. Dose difference location was evaluated using dose-location histogram. RESULTS: Calculation grid resolution significantly impacted electron dose distribution (p < 0.01), where the finest grid (0.15 cm) showed highest similarity to stored doses. CT-calibration curve and MC-history number had a negligible influence on dose reconstruction. Dosimetric difference between reconstructed and stored doses was < 1 Gy for breast and tumour bed. Reconstructed dose was achieved > 90% gamma passing rate in the validation set. However, around 2.5 Gy dose differences were observed at the skin and tissue interface regions. CONCLUSIONS: Retrospective electron boost dose reconstruction is feasible with acceptable accuracy, and could increase data completeness in large cohort studies. Caution is advised when assessing dose near tissue interface and further validation is needed outside the REQUITE dataset.
Multicomponent arrays based on a central iridium(III) bis-terpyridine complex (Ir) used as assembling metal and free-base, zinc(II) or gold(III) tetraaryl-porphyrins (PH(2), PZn, PAu) have been designed to generate intramolecular photoinduced charge separation. The rigid dyads PH(2)-Ir, PZn-Ir, PAu-Ir, and the rigid and linear triads PH(2)-Ir-PAu, PZn-Ir-PAu, as well as the individual components Ir, PH(2), PZn, PAu have been synthesized and characterized by various techniques including electrochemistry. Their photophysical properties either in acetonitrile or in dichloromethane and toluene have been determined by steady-state and time-resolved methods. In acetonitrile, excitation of the triad PH(2)-Ir-PAu leads to a charge separation with an efficiency of 0.5 and a resulting charge-separated (CS) state with a lifetime of 3.5 ns. A low-lying triplet localized on PH(2) and the presence of the heavy Ir(III) ion offer the CS state an alternative deactivation path through the triplet state. The behavior of the triad PZn-Ir-PAu in dichloromethane is rather different from that of PH(2)-Ir-PAu in acetonitrile since the primary electron transfer to yield PZn(+)()-Ir(-)-PAu is not followed by a secondary electron transfer. In this solvent, both unfavorable thermodynamic and electronic parameters contribute to the inefficiency of the second electron-transfer reaction. In contrast, in toluene solutions, the triad PZn-Ir-PAu attains a CS state with a unitary yield and a lifetime of 450 ns. These differences can be understood in terms of ground-state charge-transfer interactions as well as different stabilization of the intermediate and final CS states by solvent.
We consider the electron transfer along helical forms of proteins. The spatial structure of the protein helices is modeled by three-dimensional oscillator networks whose constituents represent peptide groups. Covalent and hydrogen bonds between the peptide units are modeled by point-point interaction potentials. The electronic degree of freedom is described by a tight-binding system including besides the nearest-neighbor exchange interactions between covalently connected units also third- or fourth-nearest neighbor interactions between hydrogen-bonded sites. In addition each peptide unit possesses an internal vibrational degree of freedom. The various dynamical degrees of freedom are coupled to each other making the exchange of electronic, intramolecular, and bond-vibrational energy possible. In the first part of the paper we investigate the static polaron formation resulting from strong interactions between the electron and the intramolecular vibrations. The 3-10 helix and the alpha helix are investigated. Polaron states are constructed analytically on the basis of a variational approach. Compared to the alpha helix the 3-10 helix supports stronger localized polarons. In the second part of the paper we take the coupling of the polaron with the vibrations of the three-dimensional protein matrix into account focusing interest on the bond-assisted initiation of polaron motion. In detail it is demonstrated that the interplay of the protein matrix and the polaron dynamics conspire to activate not only the polaron motion but also to maintain a long-lived coherently traveling localized pattern along the lattice of peptide units. Starting from a nonequilibrium state it is shown that coexisting electron and bond-vibration breathers assist the relaxation dynamics towards energy equilibration and the attainment of a stationary regime.