![]() ![]() Generally, the precursor of caspase-3 in cells is incompetent. The CPF peptides show potential for development into agents for the treatment of Type 2 diabetes.Ĭopyright © 2012 Elsevier Masson SAS. METHODS: AP was induced by 4 intraperitoneal injections of caerulein at 1 h intervals. The mechanism of action of the CPF peptides involves, at least in part, membrane depolarization and an increase in intracellular Ca(2+) concentration. No CPF peptide stimulated release of the cytosolic enzyme, lactate dehydrogenase from BRIN-BD11 cells at concentrations up to 3 μM indicating that the integrity of the plasma membrane had been preserved. Caerulein precursor fragment (CPF) peptides from the skin secretions of Xenopus laevis and Silurana epitropicalis are potent insulin-releasing agents. In addition, CPF-SE1 (GFLGPLLKLGLKGVAKVIPHLIPSRQQ), previously isolated from skin secretions of the tetraploid frog Silurana epitropicalis, produced a significant (P < 0.05) increase in the rate of insulin release at 0.03 nM with a 514 ± 13% increase over basal rate at 3 μM. In addition, CPF-SE1 (GFLGPLLKLGLKGVAKVIPHLIPSRQQ), previously isolated from skin secretions of the tetraploid frog Silurana epitropicalis, produced a significant (P <0. Primary structures of the caerulein precursor fragment (CPF) peptides isolated from skin secretions of frogs belonging to the genera Xenopus and. Partial structures of the two different caerulein precursors. CPF-7 (GFGSFLGKALKAALKIGANALGGAPQQ) produced the maximum stimulation of insulin release (571 ± 30% of basal rate at 3 μM). Peptide CPF-B1: Has antimicrobial activity against Gram-negative bacteria E.coli ATCC 25922 (MIC5 uM) and multidrug-resistant A.baumannii (MIC4-8 uM). region coding for the fragment Trp-Met-Asp-Pheof caerulein. CPF-1, CPF-3, CPF-5 and CPF-6 were the most potent producing a significant (P < 0.05) increase in the rate of insulin release at concentration of 0.03 nM. Caerulein is processed from preprocaerulein, which also contains an antimicrobial peptide called the caerulein precursor fragment. We also provide custom peptide synthesis, process development, GMP manufacturing. These peptides were purified to near homogeneity and structural characterization showed that they belong to the magainin (2 peptides), peptide glycine-leucine-amide (PGLa) (1 peptide), xenopsin precursor fragment (1 peptide), and caerulein precursor fragment (CPF) (6 peptides) families. As the main model for our study, we used a peptide pair composed of the systemic toxin caerulein, and the AMP caerulein precursor fragment-3 (CPF), both of which are key constituents of the skin. Creative Peptides offers Caerulein precursor-related fragment Ea for your research. precursor sequences share a region divided over exons 2 and 3. These are Arg-Arg-Phe-Ala-Asp-Gly or Arg-Arg-Asp-Gly at the amino-terminal side and Gly- Arg-Arg at the carboxyl end. precursor fragment, the HLP caerulein and the AMP caerulein precursor fragment 5,25,29. All rights reserved.Peptidomic analysis of norepinephrine-stimulated skin secretions of the tetraploid clawed frog Xenopus laevis (Pipidae) led to the identification of 10 peptides with the ability to stimulate the release of insulin from the rat BRIN-BD11 clonal β cell line. In the homologous precursor polypeptides deduced from the nucleotide sequence of these cloned cDNAs, the caerulein copies are flanked bycomplex processing sequences. The most abundant antimicrobial peptide in the secretions, CPF-C1 (GFGSLLGKALRLG ANVL.NH(2)) inhibited the growth of the Gram-negative bacteria Acinetobacter baumannii, Klebsiella pneumoniae, and Pseudomonas aeruginosa (MIC≤25μM) suggesting potential for development into an anti-infective agent for use against these emerging antibiotic-resistant pathogens.Ĭopyright © 2010 Elsevier Inc. Caerulein precursor fragment (CPF) peptides from the skin secretions of Xenopus laevis and Silurana epitropicalis are potent insulin-releasing agents. The magainins and the XPF peptide were active only against the Gram-negative microorganism Escherichia coli whereas the CPF peptides were also active against the Gram-positive Staphylococcus aureus. Characterization of the peptides demonstrated that they are structurally similar to magainins (2 peptides), caerulein-precursor fragments, CPF (2 peptides), and xenopsin-precursor fragments, XPF (1 peptide) that have been previously isolated from other species of the genus Xenopus. Five peptides with antimicrobial activity were isolated from norepinephrine-stimulated skin secretions of the tetraploid frog Xenopus clivii Peracca, 1898 (Pipidae). ![]()
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