RESUMO
PURPOSE: To evaluate the neutron and photon dose equivalent rate (H(n,D) and H(G)) at the outer maze entrance and the adjacent treatment console area after the installation of a Varian Clinac 23EX accelerator with a higher beam energy than its predecessor. The evaluation was based on measurements and comparison with several empirical calculations. The effectiveness of borated polyethylene (BPE) boards, as a maze wall lining material, on neutron dose and photon dose reduction is also reported. METHODS: A single energy Varian 6 MV photon linear accelerator (linac) was replaced with a Varian Clinac 23EX accelerator capable of producing 18 MV photons in a vault originally designed for the former accelerator. In order to evaluate and redesign the shielding of the vault, the neutron dose equivalent H(n,D) was measured using an Andersson-Braun neutron Rem meter and the photon dose equivalent HG was measured using a Geiger Müller and an ion chamber gamma-ray survey meter at the outer maze entrance. The measurement data were compared to semiempirical calculations such as the Kersey method, the modified Kersey method, and a newly proposed method by Falcão et al. Additional measurements were taken after BPE boards were installed on the maze walls as a neutron absorption lining material. RESULTS: With the gantry head tilted close to the inner maze entrance and with the jaws closed, both neutron dose equivalent and photon dose equivalent reached their maximum. Compared to the measurement results, the Kersey method overestimates the neutron dose equivalent H(n,D) by about two to four times (calculation/measurement ratio approximately 2.4-3.8). Falcão's method largely overestimates the H(n,D) (calculation/measurement ratio approximately 3.9-5.5). The modified Kersey method has a calculation to measurement ratio about 0.6-0.9. The photon dose equivalent calculation including McGinley's capture gamma dose equivalent equation estimates about 77%-98% of the measurement. After applying BPE boards as a lining material on the inner corner of the maze wall, the H(n,D) and the H(G) at maze entrance were decreased by 41% and 59%, respectively. CONCLUSIONS: This work indicates that the Kersey method overestimates the neutron dose equivalent H(n,D) for a Varian Clinac 23EX accelerator. The Falcão method overestimates the H(n,D) partially due to the discrepancy in the International Commission on Radiological Protection (ICRP) conversion factors caused by the uncertainties of the estimated average neutron energy. The modified Kersey method gives the closest estimation of a Varian Clinac 23EX accelerator operated at 18 MV photon mode in a maze with a similar design as in the authors' study. However, it should be used with caution because of its tendency to underestimate the H(n,D). A borated polyethylene lining can provide a cost effective method to reduce neutron and photon dose equivalent at the maze door for an existing linac vault, following the installation of a higher energy linac.
Assuntos
Nêutrons , Doses de Radiação , Proteção Radiológica/instrumentação , Boro/química , Nêutrons/uso terapêutico , Aceleradores de Partículas , Fótons/uso terapêutico , Polietileno/químicaRESUMO
Megavoltage X-ray sources are commonly used for therapy planning, and knowledge of their spectral distribution is important for accurate dose calculations. There are many methods that could provide reasonable estimations of Megavoltage X-ray spectra, when very accurate attenuation data or at least very good set of initial guesses of the spectra are available. We present here a novel method, which can be used for accurate Megavoltage spectral reconstruction without any prior knowledge of spectral distribution; the method performs well even when the available transmission data are affected by noise. The method is based on a search for a smooth function that minimizes the differences between measured and calculated attenuation data. The algorithm is compared with well-known existing algorithms, using computer simulated data, both error-free and containing added random Gaussian noise. The reconstructed spectra are subsequently used to calculate the transmission through 50 cm of bone, muscle or fat tissue. It is shown that the relative errors in dose calculations, using the spectra reconstructed via this method, are significantly smaller than those obtained via well-established reconstruction algorithms--Truncated Singular Value Decomposition (TSVD) and Expectation Maximization (EM). These results suggest that the novel algorithm might be practical for routine Megavoltage therapy X-ray source calibration.
Assuntos
Algoritmos , Processamento de Imagem Assistida por Computador/métodos , Radioterapia de Alta Energia/métodos , Análise Espectral/métodos , Raios X , Simulação por Computador , Modelos Lineares , Método de Monte Carlo , Distribuição NormalRESUMO
A molecular model is proposed to explain water 1H NMR spin-lattice relaxation at different levels of hydration (NMR titration method) on collagen. A fast proton exchange model is used to identify and characterize protein hydration compartments at three distinct Gibbs free energy levels. The NMR titration method reveals a spectrum of water motions with three well-separated peaks in addition to bulk water that can be uniquely characterized by sequential dehydration. Categorical changes in water motion occur at critical hydration levels h (g water/g collagen) defined by integral multiples N = 1, 4 and 24 times the fundamental hydration value of one water bridge per every three amino acid residues as originally proposed by Ramachandran in 1968. Changes occur at (1) the Ramachandran single water bridge between a positive amide and negative carbonyl group at h1 = 0.0658 g/g, (2) the Berendsen single water chain per cleft at h2 = 0.264 g/g, and (3) full monolayer coverage with six water chains per cleft level at h3 = 1.584 g/g. The NMR titration method is verified by comparison of measured NMR relaxation compartments with molecular hydration compartments predicted from models of collagen structure. NMR titration studies of globular proteins using the hydration model may provide unique insight into the critical contributions of hydration to protein folding.