PubMed Health⌕ Search

PubMed · 11797949

Matching tomographic IMRT fields with static photon fields.

Abstract

The matching of abutting radiation fields presents a challenging problem in radiation therapy. Due to sharp penumbra of linear accelerator beams, small (1-2 mm) errors in field positioning can lead to large (>30%) hot or cold spots in the abutment region. With head and neck immobilization devices (thermoplastic mask/aquaplast) an average setup error of 3 mm has been reported. Therefore hot or cold spots approaching 50% of the prescription dose may occur along the matchline. Although abutting radiation fields have been investigated for static fields, there is no reported study regarding matching of tomographic IMRT and static fields. Compared to static fields, the matching of tomographic IMRT fields with static fields is more complicated. Since IMRT and static fields are planned on separate treatment planning computers, the dose in the abutment region is not specified. In addition, commonly used techniques for matching fields, such as feathering of junctions, are not practical. We have developed a method that substantially reduces dose inhomogeneity in the abutment region. In this method, a "buffer zone" around the matchline was created and was included as part of the target for both IMRT and static field plans. In both fields, a small dose gradient (< or =3%/mm) in the buffer zone was created. In the IMRT plan, the buffer zone was divided into three sections with dose varying from 83% to 25% of prescription dose. The static field dose profile was modified using either a specially designed physical (hard) or a dynamic (soft) wedge. When these modified fields were matched, the combined dose in the abutment region varied by < or =10% in the presence of setup errors spanning 4 mm (+/-2 mm) when the hard wedge was used and 10 mm (+/-5 mm) with the soft wedge.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

A Sethi, L Leybovich, N Dogan, B Emami. 2001. Matching tomographic IMRT fields with static photon fields.. https://doi.org/10.1118/1.1418238

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Computational simulation of the statistical properties of unfolded proteins.

A simple Monte Carlo method was used to generate ensembles of simulated polypeptide conformations that are restricted only by steric repulsion. The models used for these simulations were based on the sequences of four real proteins, ranging in size from 26 to 268 amino acid residues, and included all non-hydrogen atoms. Two sets of calculations were performed, one that included only intra-residue steric repulsion terms and those between adjacent residues, and one that included repulsion terms between all possible atom pairs, so as to explicitly account for the excluded volume effect. Excluded volume was found to increase the average radius of gyration of the chains by 20-40%, with the expansion factor increasing with chain length. Contrary to recent suggestions, however, the excluded volume effect did not greatly restrict the distribution of dihedral angles or favor native-like topologies. The average dimensions of the ensembles calculated with excluded volume were consistent with those measured experimentally for unfolded proteins of similar sizes under denaturing conditions, without introducing any adjustable scaling factor. The simulations also reproduced experimentally determined effective concentrations for the formation of disulfide bonds in reduced and unfolded proteins. The statistically generated ensembles included significant numbers of conformations that were nearly as compact as the corresponding native proteins, as well as many that were as accessible to solvent as a fully extended chain. On the other hand, conformations with as much buried surface area as the native proteins were very rare, as were highly extended conformations. These results suggest that the overall properties of unfolded proteins can be usefully described by a random coil model and that an unfolded polypeptide can undergo significant collapse while losing only a relatively small fraction of its conformational entropy.

Biophysical Phenomena↗

The weighted-volume derivative of a space-filling diagram.

Computing the volume occupied by individual atoms in macromolecular structures has been the subject of research for several decades. This interest has grown in the recent years, because weighted volumes are widely used in implicit solvent models. Applications of the latter in molecular mechanics simulations require that the derivatives of these weighted volumes be known. In this article, we give a formula for the volume derivative of a molecule modeled as a space-filling diagram made up of balls in motion. The formula is given in terms of the weights, radii, and distances between the centers as well as the sizes of the facets of the power diagram restricted to the space-filling diagram. Special attention is given to the detection and treatment of singularities as well as discontinuities of the derivative.

Biophysical Phenomena↗

Cationic liposome-mediated gene delivery: biophysical study and mechanism of internalization.

To identify factors affecting cationic liposome-mediated gene delivery efficiency, we studied the relationship between the biophysical characteristics of liposome/DNA complexes (lipoplexes) at different (+/-) charge ratios, their structures as monitored by atomic force microscopy (AFM), and their mechanism(s) of internalization into the cells. Significant changes were observed in the particle size and zeta potential of liposomes and their structures assessed by AFM upon addition of DNA, which depended on (+/-) charge ratios. AFM images showed that lipoplexes were formed from extensively fused and apparently homogeneous lipid particles encapsulating DNA. Lipoplexes were found to internalize the cells through the endocytosis pathway. Lipoplex-cell fusion was found to occur mainly at the plasma membrane level; however, this lipoplex-cell membrane fusion was found to be essential for the uptake of the large particles. A new perspective for the internalization of large lipoplex particles into cytoplasm is discussed.

Biophysical Phenomena↗