29 research outputs found

    Synthesis of High-Molecular-Weight Poly(ether-<i>alt</i>-ester) by Selective Double Ring-Opening Polymerization of Spiroorthoesters

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    We report the selective double ring-opening polymerization of presequenced spiroorthoester monomers to form high-molecular-weight (≈90 kDa) poly­(ether-alt-ester)­s with a simple cationic alkyl gallium catalyst. The selective formation of double ring-opened polymer units was confirmed by NMR and IR spectroscopies. Thermal and rheological properties of homo- and copolymers were further characterized by differential scanning calorimetry, thermogravimetric analysis, and stress-controlled rotational rheometry. Linear viscoelastic moduli show that these systems are well entangled (plateau modulus), thereby possessing nearly terminal relaxation at long time scales (low frequencies) and Rouse segmental dynamics at short time scales (high frequencies) with characteristic slopes. These are the highest-molecular-weight poly­(ether-alt-ester)­s reported to date

    Synthesis of High-Molecular-Weight Poly(ether-<i>alt</i>-ester) by Selective Double Ring-Opening Polymerization of Spiroorthoesters

    No full text
    We report the selective double ring-opening polymerization of presequenced spiroorthoester monomers to form high-molecular-weight (≈90 kDa) poly­(ether-alt-ester)­s with a simple cationic alkyl gallium catalyst. The selective formation of double ring-opened polymer units was confirmed by NMR and IR spectroscopies. Thermal and rheological properties of homo- and copolymers were further characterized by differential scanning calorimetry, thermogravimetric analysis, and stress-controlled rotational rheometry. Linear viscoelastic moduli show that these systems are well entangled (plateau modulus), thereby possessing nearly terminal relaxation at long time scales (low frequencies) and Rouse segmental dynamics at short time scales (high frequencies) with characteristic slopes. These are the highest-molecular-weight poly­(ether-alt-ester)­s reported to date

    Pro-apoptotic Bid induces membrane perturbation by inserting selected lysolipids into the bilayer

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    Bid is a BH3-only member of the Bcl-2 family that regulates cell death at the level of mitochondrial membranes. Bid appears to link the mitochondrial pathway with the death receptor-mediated pathway of cell death. It is generally assumed that the f.l. (full-length) protein becomes activated after proteolytic cleavage, especially by apical caspases like caspase 8. The cleaved protein then relocates to mitochondria and promotes membrane permeabilization, presumably by interaction with mitochondrial lipids and other Bcl-2 proteins that facilitate the release of apoptogenic proteins like cytochrome c. Although the major action may reside in the C-terminus part, tBid (cleaved Bid), uncleaved Bid also has pro-apoptotic potential when ectopically expressed in cells or in vitro. This pro-apoptotic action of f.l. Bid has remained unexplained, especially at the biochemical level. In the present study, we show that f.l. (full-length) Bid can insert specific lysolipids into the membrane surface, thereby priming mitochondria for the release of apoptogenic factors. This is most effective for lysophosphatidylcholine species that we report to accumulate in mitochondria during apoptosis induction. A Bid mutant that is not pro-apoptotic in vivo is defective in lysophosphatidylcholine-mediated membrane perturbation in vitro. Our results thus provide a biochemical explanation for the pro-apoptotic action of f.l. Bid. © 2005 Biochemical Society

    Incidence and factors associated with anemia among the geriatric population at a tertiary care hospital in southern India

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    INTRODUCTION: Anaemia in geriatric populations poses challenges to healthcare systems worldwide. Hence, this study was done to investigate the incidence of anemia among the geriatric population of South India. METHODS: Retrospective, cross-sectional study with 144 patients aged 65 years and above. Socio-demographic data and laboratory findings were recorded in a validated proforma format. Data were analyzed using SPSS. RESULTS: 36.1% of the study population was anemic, and 63.9% were non-anemic. The prevalence of anemia was higher among females (36.36%) than males (35.82%). The prevalence of anemia was significantly correlated with advanced age (r=0.21; p < 0.05) and female sex (r=0.25; p < 0.05). Thirty-six patients were mild anemic (69%), 13 had moderate (25%), and 3 (6%) had severe anemia. Nutritional anemia was most common (80%), followed by hemorrhagic anemia (18%) and hemolytic anemia (2%). Among the 52 patients who were anemic, the most common comorbidities associated were Type 2 diabetes mellitus (69.2%) and hypertension (53.8%). Liver diseases were present in 5 cases (9.62%), renal insufficiency in 14 cases (26.9%), hypercholesterolemia in 5 cases (9.62%), and 6 cases (11.5%) were associated with other diseases. All the patients were managed conservatively with treatment, and anemia improved in 36.5% of cases. CONCLUSION: Anaemia was frequently diagnosed in the studied geriatric population. Nutritional deficiencies were the most common cause, followed by hemorrhagic and hemolytic anemia. The impact of anemia on quality of life, recovery from illness, and functional abilities must be further investigated in future geriatric studies

    Analysis of MD simulation trajectories of 20 ns time scale.

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    (A) RMSD plot displaying the molecular vibration of Cα backbone of wild type (red), and G78S mutant (black). (B) RMSD plot displaying the molecular vibration of Cα backbone of wild type mitochondrial ATPase (black), and T146A mutant (red). (C) RMSF plots show the fluctuations of respective amino acids throughout the simulation time 20 ns wild type (red), and G78S mutant (black). (D) RMSF plots show the fluctuations of respective amino acids throughout the simulation time 20 ns wild type mitochondrial ATPase (black), and T146A mutant (red). (E) The radius of gyration plots for the deduction of compactness of protein wild type (red), and G78S mutant (black). (F) Radius of gyration plots for wild type mitochondrial ATPase (black), and T146A mutant (red). (G) Number of hydrogen bonds formed between G78 and chain B (red) and S78 and chain B (black) during 20 ns simulation time scale. Principal Component Analysis (PCA) of (H) wild type chain A domain and (I) G78S mutant, (J) wild type ATPase and (K) mutant T146A, into unordered (yellow) to ordered (black) clusters, while comparing PC1 and PC2 for 20 ns simulation trajectories.</p
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