PubMed · 11539708
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R Silberberg, C H Tsao, J H Adams, J R Letaw. 1987. Radiation hazards in space.. https://pubmed.ncbi.nlm.nih.gov/11539708/
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Peptide YY and neuropeptide Y are common peptides with a high degree of primary and tertiary structural homology. They are multifunctional and participate in a diverse array of distinct activities including regulation of gastrointestinal function and neural regulation of satiety. Recently both have been implicated in aluminium chemistry in vivo although their modus opperandi have not been determined. We have used molecular fluorescence, RP-HPLC, ESMS and equilibrium dialysis to identify if either peptide YY or neuropeptide Y will bind aluminium in vitro under near-physiological conditions. We were unable to demonstrate any direct interaction between either peptide and aluminium although we have speculated upon an in vivo mechanism whereby PYY, in particular, might form a stable complex with aluminium.
Near interfaces between two different media exposed to high-energy electron beams substantial dose and fluence perturbations due to backscatter can be observed. In this work, dose and fluence perturbations were studied for 4-19 MeV electron beams at backscatter interfaces of polystyrene, graphite, water, aluminium and lead. Measurements of relative dose using an NPL-designed thin-window plane-parallel ion chamber and a Markus ion chamber were performed to determine the effect of different interface materials and thicknesses. Results of Monte Carlo simulations with the EGSnrc code, including models of the ion chambers, were found to be in excellent agreement with the measurements. The well-documented increasing dose perturbation with increasing effective atomic number of the backscatter material and decreasing electron beam energy was confirmed. Simulations in a simplified slab geometry showed that, despite the decrease of average electron energy with depth in water, the dose perturbations decrease with increasing depth of the interface in water for all the materials in the study. This was ascribed to the change of the electron angular distribution with depth which has a different effect in water and in the presence of a high-Z interface. Electron fluence perturbations near a lead/water interface were found to cause small differences in unrestricted mass collision stopping power ratios, water to air. Effects of bremsstrahlung photons, characteristic photons and positrons from the backscattering material were found to be insignificant for electron interface dosimetry. When comparing simulations using EGSnrc and the older version of the same code, EGS4, underestimations of the dose perturbation effects of up to 7% were found when using the latter code to simulate 4 MeV electrons irradiating a lead/water interface. It is concluded that EGSnrc is a highly suitable tool for electron interface dosimetry studies.
The kinetics and thermodynamics of Al(III) exchange between aluminum citrate (AlL) and human serum transferrin were investigated in the 7.2-8.9 pH range. The C-site of human serum apotransferrin in interaction with bicarbonate removes Al(III) from Al citrate with an exchange equilibrium constant K1 = (2.0 +/- 0.6) x 10(-2); a direct second-order rate constant k1 = 45 +/- 3 M(-1) x s(-1); and a reverse second-order rate constant k(-1) = (2.3 +/- 0.5) x 10(3) M(-1) x s(-1). The newly formed aluminum-protein complex loses a single proton with proton dissociation constant K1a = (15 +/- 3) nM to yield a first kinetic intermediate. This intermediate then undergoes a modification in its conformation followed by two proton losses; first-order rate constant k2 = (4.20 +/- 0.02) x 10(-2) s(-1) to produce a second kinetic intermediate, which in turn undergoes a last slow modification in the conformation to yield the aluminum-loaded transferrin in its final state. This last process rate-controls Al(III) uptake by the N-site of the protein and is independent of the experimental parameters with a constant reciprocal relaxation time tau3(-1) = (6 +/- 1) x 10(-5) x s(-1). The affinities involved in aluminum uptake by serum transferrins are about 10 orders of magnitude lower than those involved in the uptake of iron. The interactions of iron-loaded transferrins with transferrin receptor 1 occur with average dissociation constants of 3 +/- 1 and 5 +/- 1 nM for the only C-site iron-loaded and of 6.0 +/- 0.6 and 7 +/- 0.5 nM for the iron-saturated ST in the absence or presence of CHAPS, respectively. No interaction is detected between receptor 1 and aluminum-saturated or mixed C-site iron-loaded/N-site aluminum-loaded transferrin under the same conditions. The fact that aluminum can be solubilized by serum transferrin in biological fluids does not necessarily imply that its transfer from the blood stream to cytoplasm follows the receptor-mediated pathway of iron transport by transferrins.