Publications by authors named "B Hargittai"
Article Synopsis
- Biocompatible tripeptide self-assembled monolayers (SAMs) were engineered with a carboxylate group to attract lysine around the cytochrome heme site, forming a specialized electroactive structure on a gold electrode.
- Exposure of the peptide/Au electrode to cytochrome led to a measured surface coverage of 11 ± 3 pmol/cm, and atomic force microscopy provided detailed images of the protein layer with minimal surface roughness.
- Electrochemical analysis showed that the protein's surface charge impacts its redox behavior, with shifts in formal potential and accelerated electron transfer rates observed for cytochrome when bound to tripeptide/Au compared to traditional SAMs.
Nociceptin, a 17 amino acid opioid-like peptide that has an inhibitory effect on synaptic transmission in the nervous system, is involved in learning, memory, attention, and emotion and is also implicated in the perception of pain and visual, auditory, and olfactory functions. In this study, we investigated the NMR solution structure of nociceptin in membrane-like environments (trifluoroethanol and SDS micelles) and found it to have a relatively stable helix conformation from residues 4-17 with functionally important N-terminal residues being folded aperidoically on top of the helix. In functional assays for receptor binding and calcium flux, alanine-scanning variants of nociceptin indicated that functionally important residues generally followed helix periodicity, consistent with the NMR structural model.
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- Many naturally occurring peptides like somatostatins and defensins feature a cysteine residue at their C-terminus, which is useful for creating antibodies through conjugation to carrier proteins.
- Challenges in solid-phase peptide synthesis can arise from low yields and issues like racemization when attaching C-terminal cysteine, but a new anchoring strategy reduces these problems by using a preformed handle derivative.
- This method successfully synthesizes several peptides, including somatostatin, while preventing undesirable changes and ensuring high yields during the release process from the support.
Based on structure-activity relationships of the angiostatic beta-sheet-forming peptide anginex, we have designed a mimetic, 6DBF7, which inhibits angiogenesis and tumor growth in mice. 6DBF7 is composed of a beta-sheet-inducing dibenzofuran (DBF)-turn mimetic and two short key amino acid sequences from anginex. This novel antiangiogenic molecule is more effective in vivo than parent anginex.
View Article and Find Full Text PDFAnginex is a novel cytokine-like peptide with potent anti-angiogenic activity, which operates specifically against angiogenically-activated endothelial cells via prevention of cell adhesion/migration on the extracellular matrix and subsequent induction of apoptosis. Here, we demonstrate that anginex inhibits tumor growth in vivo in mouse xenograft models. In the MA148 ovarian carcinoma model, tumor growth was inhibited dose-dependently by up to 80% when systemically administered via osmotic mini-pumps starting at the time of tumor cell inoculation.
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