PubMed · 1552634
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J W Severinghaus. 1992-04-15. More RIpH.. https://doi.org/10.1001/jama.1992.03480150041022
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In order to clarify the suitability of assay method, the stability of amoxycillin (AMX) in the acidic solution at pH 1.2 was determined by two different methods, ultraviolet absorption (UV) and HPLC methods. The determination was simultaneously performed for the same sample solutions. The data from HPLC method indicated that AMX degraded and the concentration of AMX in the acidic solution was decreased. The apparent first-order rate constant (k(obs)) for the degradation was 9.83x10(-2) h(-1), and the half-life was calculated to be 7.04 h. On the other hand, the data obtained from UV method apparently represented that the concentration of AMX increased with time-course. This phenomena was brought about by the increase of UV absorption at 272 nm, which accompanied with the degradation of AMX. These results clearly indicate that UV method can not be used for determining the samples accompanying the degradation of AMX. In general, the dissolution test (drug release test) has been used for the evaluation of a sustained-release dosage form of AMX. It is impossible to avoid the degradation of AMX in the test under acidic conditions. The results indicated that the UV method should not be used for the determination of AMX in the test.
Ordering particles at the nanometre length scale is a challenging and active research area in materials science. Several approaches have so far been developed, ranging from the manipulation of individual particles to the exploitation of self-assembly in colloids. Nanometre-scale ordering is well known to appear spontaneously when anisotropic organic moieties form liquid-crystalline phases; this behaviour is also observed for anisotropic mineral nanoparticles resulting in the formation of nematic, smectic and hexagonal mesophases. Here we describe a lyotropic liquid-crystalline lamellar phase comprising an aqueous dispersion of planar solid-like sheets in which all the atoms involved in a layer are covalently bonded. The spacing of these phosphatoantimonate single layers can be increased 100-fold, resulting in one-dimensional structures whose periodicity can be tuned from 1.5 to 225 nanometres. These highly organized materials can be mechanically or magnetically aligned over large pH and temperature ranges, and this property can be used to measure residual dipolar couplings for the structure determination of biomolecules by liquid-state NMR. We also expect that our approach will result in the discovery of other classes of mineral lyotropic lamellar phases.
The assembly of the beta-amyloid peptide (Abeta) into amyloid fibrils is essential to the pathogenesis of Alzheimer's disease. Detailed structural information about fibrillogenesis has remained elusive due to the highly insoluble, noncrystalline nature of the assembled peptide. X-ray fiber diffraction, infrared spectroscopy, and solid-state NMR studies performed on fibrils composed of Abeta peptides have led to conflicting models of the intermolecular alignment of beta-strands. We demonstrate here the use of photoaffinity cross-linking to determine high-resolution structural constraints on Abeta monomers within amyloid fibrils. A photoreactive Abeta(1-40) ligand was synthesized by substituting L-p-benzoylphenylalanine (Bpa) for phenylalanine at position 4 (Abeta(1-40) F4Bpa). This peptide was incorporated into synthetic amyloid fibrils and irradiated with near-UV light. SDS-PAGE of dissolved fibrils revealed the light-dependent formation of a covalent Abeta dimer. Enzymatic cleavage followed by mass spectrometric analysis demonstrated the presence of a dimer-specific ion at MH(+) = 1825.9, the predicted mass of a fragment composed of the N-terminal Abeta(1-5) F4Bpa tryptic peptide covalently attached to the C-terminal Abeta(29-40) tryptic peptide. MS/MS experiments and further chemical modifications of the cross-linked dimer led to the localization of the photo-cross-link between the ketone of the Bpa4 side chain and the delta-methyl group of the Met35 side chain. The Bpa4-Met35 intermolecular cross-link is consistent with an antiparallel alignment of Abeta peptides within amyloid fibrils.