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Facile Preparation of PNA-Peptide Conjugates with a Polar Maleimide-Thioether Linkage.

Conjugation of a delivery peptide containing a thiol functionality (e.g., a cysteine residue) with a PNA oligomer displaying a single unprotected aliphatic primary amine (e.g., the N-terminus or a C-terminal lysine residue) can be achieved via a one-pot modification with a bisfunctional maleimide linker also displaying a reactive N-hydroxysuccinimidyl ester group (e.g., Mal-PEG2-OSu). Here, an optimized protocol with respect to ratios between the reactants as well as recommended reaction times is presented. Formation and conversion of the maleimide-PNA intermediate was followed by analytical HPLC as exemplified by its conjugation to (KFF)K-Cys-NH. In addition, the reaction time required for direct conversion of a preformed Mal-(CH)-(C=O)-PNA oligomer in the presence of a slight excess of thiol-modified peptide (with a varying degree of sterical hindrance: HS-(CH)-CONH-(KFF)K-NH, (KFF)K-hCys-NH and (KFF)K-Cys-NH) is provided.

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A Plant-Specific N-terminal Extension Reveals Evolutionary Functional Divergence within Translocator Proteins.

Conserved translocator proteins (TSPOs) mediate cell stress responses possibly in a cell-type-specific manner. This work reports on the molecular function of plant TSPO and their possible evolutionary divergence. Arabidopsis thaliana TSPO (AtTSPO) is stress induced and has a conserved polybasic, plant-specific N-terminal extension. AtTSPO reduces water loss by depleting aquaporin PIP2;7 in the plasma membrane. Herein, AtTSPO was found to bind phosphoinositides in vitro, but only full-length AtTSPO or chimeric mouse TSPO with an AtTSPO N-terminus bound PI(4,5)Pin vitro and modified PIP2;7 levels in vivo. Expression of AtTSPO but not its N-terminally truncated variant enhanced phospholipase C activity and depleted PI(4,5)P from the plasma membrane and its enrichment in Golgi membranes. Deletion or point mutations within the AtTSPO N-terminus affected PI(4,5)P binding and almost prevented AtTSPO-PIP2;7 interaction in vivo. The findings imply functional divergence of plant TSPOs from bacterial and animal counterparts via evolutionary acquisition of the phospholipid-interacting N-terminus.

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Apoptosis Phospho-Specifi EGF Phospho-Specific Arra Proteins and Antibodies H Mouse Anti-Human Neuron S Anti Amyloid Precursor Pr Recombinant Rubella Viral Recombinant Human CLU Apo T-Cell Receptor Signaling Recombinant Human IFN-alp Recombinant Human AP2M1 P ACTH (N Terminal) Recombinant Human SDF-1 a

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The molecular mechanism of polymer formation of farnesylated human Guanylate Binding Protein 1.

The human guanylate binding protein 1 (hGBP1) belongs to the dynamin superfamily proteins and represents a key player in the innate immune response. Farnesylation at the C-terminus is required for hGBP1's activity against microbial pathogens as well as for its anti-proliferative and anti-tumor activity. The farnesylated hGBP1 (hGBP1) retains many characteristics of the extensively studied non-farnesylated protein and gains additional abilities like binding to lipid membranes and formation of hGBP1 polymers. These polymers are believed to serve as a protein depot making the enzyme immediately available to fight the invasion of intracellular pathogens. Here we study the molecular mechanism of hGBP1 polymer formation as it is a crucial state of this enzyme allowing for a rapid response demanded by the biological function. We employ Förster resonance energy transfer in order to trace intra- and intermolecular distance changes of protein domains. Light scattering techniques yield deep insights in the changes of size and shape. The GTP hydrolysis driven cycling between a closed, farnesyl moiety hidden state and an opened, farnesyl moiety exposed state represents a first phase, preparing the molecule for polymerization. Within the second phase of polymer growth, opened hGBP1 molecules can be incorporated in the growing polymer where the opened structure is stabilized - similar to a surfactant molecule in a micelle - pointing the farnesyl moieties into the hydrophobic center and positioning the head groups at the periphery of the polymer. We contribute the molecular mechanism of polymer formation paving the ground for a detailed understanding of hGBP1 function.

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Guanylate-binding protein Human Retinol Binding Pro DNA Binding Protein 7 (DB Mouse Anti-Human Retinol Sheep Anti-Human Retinol Recombinant Human S100B C Recombinant Human PKC the Anti Galectin(Gal 3) Huma SH3KBP1 binding protein 1 SH3 domain-binding protei DNA Binding Protein-7 (DB Goat Anti-Human Vitamin D

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