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Abstract: Alzheimer’s disease has been closely related with oxidative stress, which might be responsible for the dysfunction or death of neuronal cells that contributes to disease pathogenesis. Impaired copper homeostasis makes contribution to the oxidative stress and consequently to several neurodegenerative conditions. Inappropriate binding of Cu(II) to cellular proteins are currently being explored as sources of pathological oxidative stress in several neurodegenerative disorders. Here we report that a fragment of tau protein possesses copper reduction activity and initiates the copper-mediated generation of hydrogen peroxide. The tau peptide was found to be oxidized to form disulfide bond-linked dimer. The hydrogen peroxide generated was quantified by TCEP/DTNB (tris(2-carboxyethyl) phosphine hydrochloride/5,5′-dithio-bis(2-nitrobenzoic acid). Since the copper reduction capacity and the generation of hydrogen peroxide were believe to be a major toxicological pathway of Aβ peptide, the functional similarity shared by tau and Aβ implies a new perspective of tau pathology. [Copyright &y& Elsevier]

Abstract: Facile, mild and efficient one-pot preparation of N α-Fmoc-N ε-(benzyl, methyl)-lysine, a building block for monomethylated peptide synthesis, was described. This building block was proved to be efficient for the synthesis of site-specifically monomethylated peptide. Benzyl group, which was incorporated by reductive benzylation and removed via catalytic hydrogenolysis, served as an excellent protecting group. [Copyright &y& Elsevier]

• The dynamic model of long-span arch bridges conducted by the cantilever construction method is established. • The proposed method has excellent applicability for planner-free vibration of long-span arch bridges during construction. • The vibration of towers cannot be neglected unless it is sufficiently stiff. • The proposed model and method can be extended to the other multi-cable supported arch structures. The cantilever construction model, which consists of the arch, towers and cables, can be regarded as a cable-stayed system and is widely applied in constructing long-span arch bridges. The vibration induced by this temporary structure's unstable property has a safety risk and deserves to be concerned. Thus, a fully analytical beam-spring-arch model is presented for the cantilever and closure construction states of long-span arch bridges. Subsequently, based on the boundary and continuity conditions, the governing differential equations for in-plane free vibration are derived according to the Hamilton principle and solved using the transfer matrix method to determine frequencies and mode shapes of the system. Meanwhile, the results calculated by the proposed method are verified with the finite element method. Finally, the effects of structural parameter variations during construction on in-plane vibration properties are investigated. The results show that as the length of the erected arch rib gets longer, the system's first six-order frequencies and mode shapes are significantly affected. Moreover, the veering phenomenon is observed. The cables can increase the frequencies of the system to a certain extent. The model that neglects the tower's vibration would overestimate the stiffness of the erection system unless the tower's stiffness is much bigger than the arch. [ABSTRACT FROM AUTHOR]

Abstract: Proteins are targets of reactive nitrogen species such as peroxynitrite and nitrogen dioxide. Among the various amino acids in proteins, tyrosine and tryptophan residues are especially susceptible to attack by reactive nitrogen species. On the other hand, protein tyrosine phosphorylation has gained much attention in respect to cellular regulatory events and signal transduction. Peroxynitrite-mediated nitration of peptide YPPPPPW and phosphopeptide pYPPPPPW were studied at pH 7.4. The predominant nitrated products were separated and identified by reverse phase high performance liquid chromatography coupled with electrospray ionization mass spectrometry (LC-MS). The nitration sites were established by tandem electrospray ionization-mass spectrometry (LC-MS/MS). A regulatory effect of tyrosine phosphorylation/dephosphorylation on peptide nitration was observed. YPPPPPW was predominantly nitrated at tyrosine residue while pYPPPPPW was nitrated at tryptophan one. Our results can help in understanding the biochemical significance of the relationship of tyrosine phosphorylation and nitration in proteins. [Copyright &y& Elsevier]