A Remarkably Stable and Simple Monocyclic Thiepin. Synthesis and Properties of 2, 7-Di-tert-butyl-4-ethoxycarbonyl-5-methylthiepin

A simple monocyclic 8n electron thiepin, 2,7-di-tert-butyl-4- -ethoxycarbonyl-5-methylthiepin (13) stabilized by two bulky tert- -butyl groups at 2- and 7-positions, was synthesized from 2,6-di- -tert-butyl-4-methylthiopyrylium tetrafluoroborate (11). In spite of of its monocyclic thiepin structure, the compound 13 showed remarkable thermal stability and had a half-life of 7.1 h at 130 °C. Judging from the 1H-NMR spectrum, the thiepin 13 is considered to be an atropic molecule. Synthetic details of 11 and 13, and the chemical and physical properties of 13 are also described

Quantitative TEM imaging of the magnetostructural and phase transitions in FeRh thin film systems

Equi-atomic FeRh is a very interesting material as it undergoes a magnetostructural transition from an antiferromagnetic (AF) to a ferromagnetic (FM) phase between 75-105 °C. Its ability to present phase co-existence separated by domain walls (DWs) above room temperature provides immense potential for exploitation of their DW motion in spintronic devices. To be able to effectively control the DWs associated with AF/FM coexistence in FeRh thin films we must fully understand the magnetostructural transition and thermomagnetic behaviour of DWs at a localised scale. Here we present a transmission electron microscopy investigation of the transition in planar FeRh thin-film samples by combining differential phase contrast (DPC) magnetic imaging with in situ heating. We perform quantitative measurements from individual DWs as a function of temperature, showing that FeRh on NiAl exhibits thermomagnetic behaviour consistent with the transition from AF to FM. DPC imaging of an FeRh sample with HF-etched substrate reveals a state of AF/FM co-existence and shows the transition from AF to FM regions proceeds via nucleation of small vortex structures, which then grow by combining with newly nucleated vortex states into larger complex magnetic domains, until it is in a fully-FM state

Potent Anti-Tumor Effect Generated by a Novel Human Papillomavirus (HPV) Antagonist Peptide Reactivating the pRb/E2F Pathway

Human papillomavirus type 16 (HPV16) E7 is a viral oncoprotein believed to play a major role in cervical cancer. In this study, an antagonist peptide against HPV16E7 protein was first identified from screening the c7c phage display peptide library. The binding specificity and affinity of the selected peptide to HPV16E7 were tested by competitive enzyme-linked immunosorbent assay (ELISA). The antagonist peptide showed obvious anti-tumor efficacy both in cell lines and animal tumor models. Significant cell proliferation inhibition with high specificity was noted when HPV16-positive cells were treated with the peptide. This anti-tumor efficacy was resulted from overriding the activities of HPV16E7 and reactivating the pRb/E2F pathway, as shown by a series of experiments. Flow cytometry analysis revealed that the selected peptide induced G1 arrest in a dose-dependent manner. Competitive ELISA, pull down, and Co-IP experiments indicated that the selected peptide disrupted the interaction between HPV16E7 and pRb proteins both in vitro and in vivo. Luciferase reporter assay verified that transcription activities of E2F were suppressed by the peptide through restoration of pRb. RT-PCR and Western blot revealed that it reduced cyclins A, D1, and E1 expression, and led to HPV16E7 protein degradation, but pRb protein stabilization. The current study suggests that this specific peptide may serve as a potential therapeutic agent for HPV16-positive cervical cancer

Immune response to gut escherichia coli and susceptibility to adjuvant arthritis in the rats

We have investigated the humoral immune response to antigens of predominant gut aerobic bacterial strains (i.e. Escherichia coli) over the course of adjuvant arthritis and oil-induced arthritis in two inbred rat strains: Dark Agouti (DA) and Albino Oxford (AO). We report the presence of antibodies specific to proteins of Escherichia coli in molecular weight range between 20-30 kDa in sera of diseased DA rats, and the absence of these antibodies in the sera of AO rats. In DA rats, CFA and IFA provoked a stronger antibody response to Escherichia coli, especially of the IgG2b antibody class. Intramuscular administration of Escherichia coli preceding the adjuvant arthritis induction had no effect on the development and course of disease, as well as on the activation of T cells in the draining inguinal lymph nodes. Higher serum levels of natural and induced IgA antibodies, combined with a higher CD3(+)CD26(+) cell percentage were found in AO rats. The observed correlation between the serologic response to commensal flora and rats' genetic background as a defining factor for arthritis susceptibility may contribute to the process of creating a favorable (or less favorable) milieu for arthritis development