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Relevant bibliographies by topics / Octapeptide c terminal

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Academic literature on the topic 'Octapeptide c terminal'

Author: Grafiati

Published: 4 June 2021

Last updated: 10 February 2022

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Journal articles on the topic "Octapeptide c terminal"

1

Yu, Kun-Hua, Mei-Yu Huang, Yi-Ru Lee, Yu-Kie Lin, Hau-Ren Chen, and Cheng-I. Lee. "The Effect of Octapeptide Repeats on Prion Folding and Misfolding." International Journal of Molecular Sciences 22, no. 4 (2021): 1800. http://dx.doi.org/10.3390/ijms22041800.

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Misfolding of prion protein (PrP) into amyloid aggregates is the central feature of prion diseases. PrP has an amyloidogenic C-terminal domain with three α-helices and a flexible tail in the N-terminal domain in which multiple octapeptide repeats are present in most mammals. The role of the octapeptides in prion diseases has previously been underestimated because the octapeptides are not located in the amyloidogenic domain. Correlation between the number of octapeptide repeats and age of onset suggests the critical role of octapeptide repeats in prion diseases. In this study, we have investigated four PrP variants without any octapeptides and with 1, 5 and 8 octapeptide repeats. From the comparison of the protein structure and the thermal stability of these proteins, as well as the characterization of amyloids converted from these PrP variants, we found that octapeptide repeats affect both folding and misfolding of PrP creating amyloid fibrils with distinct structures. Deletion of octapeptides forms fewer twisted fibrils and weakens the cytotoxicity. Insertion of octapeptides enhances the formation of typical silk-like fibrils but it does not increase the cytotoxicity. There might be some threshold effect and increasing the number of peptides beyond a certain limit has no further effect on the cell viability, though the reasons are unclear at this stage. Overall, the results of this study elucidate the molecular mechanism of octapeptides at the onset of prion diseases.

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RAJH, HUBERTUS M., EDWIN C. M. MARIMAN, GODEFRIDUS I. TESSER, and RUTGER J. F. NIVARD. "TRYPTOPHAN REPLACEMENT IN THE C-TERMINAL OCTAPEPTIDE OF CCK-PZ." International Journal of Peptide and Protein Research 15, no. 3 (2009): 200–210. http://dx.doi.org/10.1111/j.1399-3011.1980.tb02569.x.

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3

LOBO-HAJDU, Gisele, Hans-Peter BRAUN, Nancy ROMP, Leslie A. GRIVELL, Jan A. BERDEN, and Udo K. SCHMITZ. "Subunit VII of ubiquinol:cytochrome-c oxidoreductase from Neurospora crassa is functional in yeast and has an N-terminal extension that is not essential for mitochondrial targeting." Biochemical Journal 320, no. 3 (1996): 769–75. http://dx.doi.org/10.1042/bj3200769.

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cDNA clones encoding subunit VII of the Neurospora crassa bc1 complex (ubiquinol:cytochrome-c oxidoreductase), which is homologous with subunit VIII of the complex from yeast (encoded by QCR8), were identified on the basis of functional complementation of a yeast QCR8 deletion strain. The clones contain an open reading frame encoding a protein with a calculated molecular mass of 11.8 kDa. The N-terminal eight residues of the amino acid sequence deduced from the cDNA clones are absent from the mature protein, as revealed by direct sequencing of the isolated protein. To investigate the potential role of the N-terminal octapeptide in mitochondrial targeting, constructs were made encoding the precursor and the mature form of subunit VII from Neurospora. Incubation of isolated mitochondria with the two proteins revealed that the N-terminal extension of the precursor is removed on import. However, the presequence does not encode information for targeting, as the proteins encoded by both constructs can be imported into isolated mitochondria with equal efficiency. In contrast, the octapeptide seems to have functional importance: the defect in the yeast qcr8-null mutant is not complemented on transformation with the construct encoding mature subunit VII from N. crassa in a single-copy plasmid. We therefore speculate that the N-terminal extension plays a role in intramitochondrial sorting of N. crassa subunit VII. This is supported by the fact that the subunit VII precursor is processed by a protease other than the general mitochondrial processing peptidase. Interestingly, the presequence of N. crassa subunit VII has an amino acid composition similar to the octapeptides cleaved off by the mitochondrial intermediate peptidase.

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4

Isaya, G., F. Kalousek, W. A. Fenton, and L. E. Rosenberg. "Cleavage of precursors by the mitochondrial processing peptidase requires a compatible mature protein or an intermediate octapeptide." Journal of Cell Biology 113, no. 1 (1991): 65–76. http://dx.doi.org/10.1083/jcb.113.1.65.

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Many precursors of mitochondrial proteins are processed in two successive steps by independent matrix peptidases (MPP and MIP), whereas others are cleaved in a single step by MPP alone. To explain this dichotomy, we have constructed deletions of all or part of the octapeptide characteristic of a twice cleaved precursor (human ornithine transcarbamylase [pOTC]), have exchanged leader peptide sequences between once-cleaved (human methylmalonyl-CoA mutase [pMUT]; yeast F1ATPase beta-subunit [pF1 beta]) and twice-cleaved (pOTC; rat malate dehydrogenase (pMDH); Neurospora ubiquinol-cytochrome c reductase iron-sulfur subunit [pFe/S]) precursors, and have incubated these proteins with purified MPP and MIP. When the octapeptide of pOTC was deleted, or when the entire leader peptide of a once-cleaved precursor (pMUT or pF1 beta) was joined to the mature amino terminus of a twice-cleaved precursor (pOTC or pFe/S), no cleavage was produced by either protease. Cleavage of these constructs by MPP was restored by re-inserting as few as two amino-terminal residues of the octapeptide or of the mature amino terminus of a once-cleaved precursor. We conclude that the mature amino terminus of a twice-cleaved precursor is structurally incompatible with cleavage by MPP; such proteins have evolved octapeptides cleaved by MIP to overcome this incompatibility.

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5

Jarrousse, C., H. Niel, M. P. Audousset-Puech, J. Martinez, and D. Bataille. "Oxyntomodulin and its C-terminal octapeptide inhibit liquid meal-stimulated acid secretion." Peptides 7 (January 1986): 253–56. http://dx.doi.org/10.1016/0196-9781(86)90196-8.

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6

Jarrousse, Claire, Marie-Pascale Audousset-Puech, Marcelle Dubrasquet, Huguette Niel, Jean Martinez, and Dominique Bataille. "Oxyntomodulin (glucagon-37) and its C-terminal octapeptide inhibit gastric acid secretion." FEBS Letters 188, no. 1 (1985): 81–84. http://dx.doi.org/10.1016/0014-5793(85)80879-6.

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7

Hara, Hideyuki, and Suehiro Sakaguchi. "N-Terminal Regions of Prion Protein: Functions and Roles in Prion Diseases." International Journal of Molecular Sciences 21, no. 17 (2020): 6233. http://dx.doi.org/10.3390/ijms21176233.

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The normal cellular isoform of prion protein, designated PrPC, is constitutively converted to the abnormally folded, amyloidogenic isoform, PrPSc, in prion diseases, which include Creutzfeldt-Jakob disease in humans and scrapie and bovine spongiform encephalopathy in animals. PrPC is a membrane glycoprotein consisting of the non-structural N-terminal domain and the globular C-terminal domain. During conversion of PrPC to PrPSc, its 2/3 C-terminal region undergoes marked structural changes, forming a protease-resistant structure. In contrast, the N-terminal region remains protease-sensitive in PrPSc. Reverse genetic studies using reconstituted PrPC-knockout mice with various mutant PrP molecules have revealed that the N-terminal domain has an important role in the normal function of PrPC and the conversion of PrPC to PrPSc. The N-terminal domain includes various characteristic regions, such as the positively charged residue-rich polybasic region, the octapeptide repeat (OR) region consisting of five repeats of an octapeptide sequence, and the post-OR region with another positively charged residue-rich polybasic region followed by a stretch of hydrophobic residues. We discuss the normal functions of PrPC, the conversion of PrPC to PrPSc, and the neurotoxicity of PrPSc by focusing on the roles of the N-terminal regions in these topics.

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8

Monk, Brian C., Kyoko Niimi, Susan Lin, et al. "Surface-Active Fungicidal d-Peptide Inhibitors of the Plasma Membrane Proton Pump That Block Azole Resistance." Antimicrobial Agents and Chemotherapy 49, no. 1 (2005): 57–70. http://dx.doi.org/10.1128/aac.49.1.57-70.2005.

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ABSTRACT A 1.8-million-member d-octapeptide combinatorial library was constructed in which each member comprised a diversity-containing N-terminal pentapeptide and a C-terminal amidated triarginine motif. The C-terminal motif concentrated the library members at the fungal cell surface. A primary screen for inhibitors of Saccharomyces cerevisiae and Candida albicans growth, together with an in vitro secondary screen with the S. cerevisiae plasma membrane ATPase (Pma1p) as a target, identified the antifungal d-octapeptide BM0 (d-NH2-RFWWFRRR-CONH2). Optimization of BM0 led to the construction of BM2 (d-NH2-RRRFWWFRRR-CONH2), which had broad-spectrum fungicidal activity against S. cerevisiae, Candida species, and Cryptococcus neoformans; bound strongly to the surfaces of fungal cells; inhibited the physiological activity of Pma1p; and appeared to target Pma1p, with 50% inhibitory concentrations in the range of 0.5 to 2.5 μM. At sub-MICs (<5 μM), BM2 chemosensitized to fluconazole (FLC) S. cerevisiae strains functionally hyperexpressing fungal lanosterol 14α-demethylase and resistance-conferring transporters of azole drugs. BM2 chemosensitized to FLC some FLC-resistant clinical isolates of C. albicans and C. dubliniensis and chemosensitized to itraconazole clinical isolates of C. krusei that are intrinsically resistant to FLC. The growth-inhibitory concentrations of BM2 did not cause fungal cell permeabilization, significant hemolysis of red blood cells, or the death of cultured HEp-2 epithelial cells. BM2 represents a novel class of broad-spectrum, surface-active, Pma1p-targeting fungicides which increases the potencies of azole drugs and circumvents azole resistance.

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9

GILLESSEN, DIETER, ARNOLD TRZECIAK, RITA K. M. MÜLLER, and ROLF O. STUDER. "SYNTHESES AND BIOLOGICAL ACTIVITIES OF METHOXININE-ANALOGUES OF THE C-TERMINAL OCTAPEPTIDE OF CHOLECYSTOKININ-PANCREOZYMIN." International Journal of Peptide and Protein Research 13, no. 2 (2009): 130–36. http://dx.doi.org/10.1111/j.1399-3011.1979.tb01860.x.

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10

Dubrasquet, J. M., M. P. Audousset-Puech, J. Martinez, and D. Bataille. "Somatostatin enhances the inhibitory effect of oxyntomodulin and its C-terminal octapeptide on acid secretion." Peptides 7 (January 1986): 257–59. http://dx.doi.org/10.1016/0196-9781(86)90197-x.

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Dissertations / Theses on the topic "Octapeptide c terminal"

1

Ferroudji, Sai͏̈d. "Effet inhibiteur de l'octapeptide C-terminal de l'oxyntomoduline sur la sécrétion acide gastrique stimulée par la pentagastrine chez l'homme : essai d'étude dose-effet." Montpellier 1, 1990. http://www.theses.fr/1990MON11196.

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2

Bouron, Estelle. "Synthèse asymétrique de lactames en série pipérazine. Application à la préparation d'analogues peptidiques de l'ODN." Rouen, 2000. http://www.theses.fr/2000ROUES063.

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Le Diazepam-binding-inhibitor (DBI) est un polypeptide de 86 acides aminés, isolé du cerveau de rat pour sa capacité à déplacer le diazepam de ses sites de liaison. Le terme général d'endozépine a été utilisé pour designer le DBI et ses fragments biologiquement actifs dont l'octadécaneuropeptide DBI 33 - 50 (ODN). Les endozépines sont impliquées dans de nombreux processus biologiques. En particulier, l'ODN augmente la concentration de calcium intracellulaire dans les astrocytes de rat lorsqu'il se lie à un recepteur membranaire couplé a une protéine G. L'étude des relations structure-activité d'une série d'analogues de synthèse de l'ODN a permis de démontrer que l'octapeptide C-terminal (H-Arg-Pro-Gly-Leu-Leu-Asp-Leu-Lys-OH) possède une activité égale à celle de l'ODN. La suite de ces études a montré que la cyclisation de cet octapeptide par les extrémités N- et C- terminales potentialise l'activité biologique du peptide, ce qui laisse supposer qu'une rigidification de la structure de la molécule favorise son activité. La modélisation moléculaire sous contrainte RMN a permis d'identifier deux éléments structuraux qui expliquent la conformation : un coude β mettant en jeu l'enchaînement -Leu-Asp-Leu-Lys- et un coude γ sur l'enchaînement -Pro-Gly-Leu-. Notre laboratoire a développé la synthèse de composés oxopipérazines afin de mimer ces coudes β et γ. Leur intégration dans l'octapeptide linéaire puis leur analyse RMN ont été effectuées et des tests biologiques in vitro réalisés.

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