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Academic literature on the topic 'Acidic oligopeptides'

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Published: 10 December 2022
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Journal articles on the topic "Acidic oligopeptides"

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Ishizaki, Junko, Yoshihiro Waki, Tatsuo Takahashi-Nishioka, Koichi Yokogawa, and Ken-ichi Miyamoto. "Selective drug delivery to bone using acidic oligopeptides." Journal of Bone and Mineral Metabolism 27, no. 1 (November 19, 2008): 1–8. http://dx.doi.org/10.1007/s00774-008-0004-z.

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Morty, Rory E., Vilmos Fülöp, and Norma W. Andrews. "Substrate Recognition Properties of Oligopeptidase B from Salmonella enterica Serovar Typhimurium." Journal of Bacteriology 184, no. 12 (June 15, 2002): 3329–37. http://dx.doi.org/10.1128/jb.184.12.3329-3337.2002.

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ABSTRACT Oligopeptidase B (OpdB) is a serine peptidase broadly distributed among unicellular eukaryotes, gram-negative bacteria, and spirochetes which has emerged as an important virulence factor and potential therapeutic target in infectious diseases. We report here the cloning and expression of the opdB homologue from Salmonella enterica serovar Typhimurium and demonstrate that it exhibits amidolytic activity exclusively against substrates with basic residues in P1. While similar to its eukaryotic homologues in terms of substrate specificity, Salmonella OpdB differs significantly in catalytic power and inhibition and activation properties. In addition to oligopeptide substrates, restricted proteolysis of histone proteins was observed, although no cleavage was seen at or near residues that had been posttranslationally modified or at defined secondary structures. This supports the idea that the catalytic site of OpdB may be accessible only to unstructured oligopeptides, similar to the closely related prolyl oligopeptidase (POP). Salmonella OpdB was employed as a model enzyme to define determinants of substrate specificity that distinguish OpdB from POP, which hydrolyzes substrates exclusively at proline residues. Using site-directed mutagenesis, nine acidic residues that are conserved in OpdBs but absent from POPs were converted to their corresponding residues in POP. In this manner, we identified a pair of glutamic acid residues, Glu576 and Glu578, that define P1 specificity and direct OpdB cleavage C terminal to basic residues. We have also identified a second pair of residues, Asp460 and Asp462, that may be involved in defining P2 specificity and thus direct preferential cleavage by OpdB after pairs of basic residues.
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Varga, V., R. Janáky, K. M. Marnela, J. Gulyás, P. Kontro, and S. S. Oja. "Displacement of excitatory amino acid receptor ligands by acidic oligopeptides." Neurochemical Research 14, no. 12 (December 1989): 1223–27. http://dx.doi.org/10.1007/bf00965513.

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Imamura, Koreyoshi, Yuuki Kawasaki, Takeshi Nagayasu, Takaharu Sakiyama, and Kazuhiro Nakanishi. "Adsorption characteristics of oligopeptides composed of acidic and basic amino acids on titanium surface." Journal of Bioscience and Bioengineering 103, no. 1 (January 2007): 7–12. http://dx.doi.org/10.1263/jbb.103.7.

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IENAGA, KAZUHARU, KO NAKAMURA, KUNIHIKO HIGASHIURA, YOSHIO TOYOMAKI, and HIROSHI KIMURA. "Simple peptides. III. Syntheses and properties of taurine-oligopeptides containing an acidic .ALPHA.-amino acid." CHEMICAL & PHARMACEUTICAL BULLETIN 36, no. 8 (1988): 2796–801. http://dx.doi.org/10.1248/cpb.36.2796.

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Mosrin, C., M. Riva, M. Beltrame, E. Cassar, A. Sentenac, and P. Thuriaux. "The RPC31 gene of Saccharomyces cerevisiae encodes a subunit of RNA polymerase C (III) with an acidic tail." Molecular and Cellular Biology 10, no. 9 (September 1990): 4737–43. http://dx.doi.org/10.1128/mcb.10.9.4737-4743.1990.

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The RPC31 gene encoding the C31 subunit of Saccharomyces cerevisiae RNA polymerase C (III) has been isolated, starting from a C-terminal fragment cloned on a lambda gt11 library. It is unique on the yeast genome and lies on the left arm of chromosome XIV, very close to a NotI site. Its coding sequence perfectly matches the amino acid sequence of two oligopeptides prepared from purified C31. It is also identical to the ACP2 gene previously described as encoding an HMG1-like protein (W. Haggren and D. Kolodrubetz, Mol. Cell. Biol. 8:1282-1289, 1988). Thus, ACP2 and RPC31 are allelic and encode a subunit of RNA polymerase C. The c31 protein has a highly acidic C-terminal tail also found in several other chromatin-interacting proteins, including animal HMG1. Outside this domain, however, there is no appreciable homology to any known protein. The growth phenotypes of a gene deletion, of insertions, and of nonsense mutations indicate that the C31 protein is strictly required for cell growth and that most of the acidic domain is essential for its function. Random mutagenesis failed to yield temperature-sensitive mutants, but a slowly growing mutant was constructed by partial suppression of a UAA nonsense allele of RPC31. Its reduced rate of tRNA synthesis in vivo relative to 5.8S rRNA supports the hypothesis that the C31 protein is a functional subunit of RNA polymerase C.
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Mosrin, C., M. Riva, M. Beltrame, E. Cassar, A. Sentenac, and P. Thuriaux. "The RPC31 gene of Saccharomyces cerevisiae encodes a subunit of RNA polymerase C (III) with an acidic tail." Molecular and Cellular Biology 10, no. 9 (September 1990): 4737–43. http://dx.doi.org/10.1128/mcb.10.9.4737.

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The RPC31 gene encoding the C31 subunit of Saccharomyces cerevisiae RNA polymerase C (III) has been isolated, starting from a C-terminal fragment cloned on a lambda gt11 library. It is unique on the yeast genome and lies on the left arm of chromosome XIV, very close to a NotI site. Its coding sequence perfectly matches the amino acid sequence of two oligopeptides prepared from purified C31. It is also identical to the ACP2 gene previously described as encoding an HMG1-like protein (W. Haggren and D. Kolodrubetz, Mol. Cell. Biol. 8:1282-1289, 1988). Thus, ACP2 and RPC31 are allelic and encode a subunit of RNA polymerase C. The c31 protein has a highly acidic C-terminal tail also found in several other chromatin-interacting proteins, including animal HMG1. Outside this domain, however, there is no appreciable homology to any known protein. The growth phenotypes of a gene deletion, of insertions, and of nonsense mutations indicate that the C31 protein is strictly required for cell growth and that most of the acidic domain is essential for its function. Random mutagenesis failed to yield temperature-sensitive mutants, but a slowly growing mutant was constructed by partial suppression of a UAA nonsense allele of RPC31. Its reduced rate of tRNA synthesis in vivo relative to 5.8S rRNA supports the hypothesis that the C31 protein is a functional subunit of RNA polymerase C.
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Nakata, Takashi, Masatoshi Takahashi, Masaru Nakatani, Rie Kuramitsu, Masahiro Tamura, and Hideo Okai. "Role of Basic and Acidic Fragments in Delicious Peptides (Lys-Gly-Asp Glu-Glu-Ser-Leu-Ala) and the Taste Behavior of Sodium and Potassium Salts in Acidic Oligopeptides." Bioscience, Biotechnology, and Biochemistry 59, no. 4 (January 1995): 689–93. http://dx.doi.org/10.1271/bbb.59.689.

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Song, L., M. Ye, M. Troyanovskaya, E. Wilk, S. Wilk, and D. P. Healy. "Rat kidney glutamyl aminopeptidase (aminopeptidase A): molecular identity and cellular localization." American Journal of Physiology-Renal Physiology 267, no. 4 (October 1, 1994): F546—F557. http://dx.doi.org/10.1152/ajprenal.1994.267.4.f546.

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Glutamyl aminopeptidase [aminopeptidase A (EAP), EC 3.4.11.7] is an ectoenzyme that selectively hydrolyzes acidic amino acid residues from the amino terminus of oligopeptides. EAP activity is highest within the kidney and small intestine. The murine pre-B cell BP-1/6C3 and the human kidney glycoprotein gp160 differentiation antigens have been reported to have biochemical properties indistinguishable from EAP. It is not known, however, if rat kidney EAP is a homologue of these antigens or molecularly distinct. Using the reverse transcription-polymerase chain reaction method with oligonucleotide primers based on the BP-1/6C3 nucleotide sequence, we isolated a 450-bp partial cDNA from rat kidney poly(A)+ RNA. The partial cDNA encoded a predicted protein that was 92% and 86% identical to the murine BP-1/6C3 and human gp160 antigens, respectively; the amino acid sequence within the zinc-binding domain was completely conserved. Purification of EAP from rat kidney and microsequence analysis of a tryptic digest peptide fragment (18-mer) indicated that the fragment was highly similar to a region within the BP-1/6C3 and gp160 proteins. Northern blot hybridization and immunoblot analyses were also consistent with labeling of products the same size as reported for the BP-1/6C3 and gp160 antigens. There was a good correlation between the cellular distribution of EAP mRNA and EAP immunoreactivity, with proximal tubules and glomerular mesangial cells having the highest densities. These results indicate that rat kidney EAP is a species homologue of the murine BP-1/6C3 and human gp160 antigens. Furthermore, on the basis of its cellular localization, rat kidney EAP is likely to be involved in degradation of oligopeptides within the glomerulus and the glomerular filtrate. Since cells that express EAP also express receptors for angiotensin II, an intrarenal vasoactive hormone that is a substrate for EAP, these results further suggest that EAP may play a role in modulating the activity of intrarenal angiotensin II.
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Görnhardt, Birgit, Ila Rouhara, and Elmon Schmelzer. "Cyst Germination Proteins of the Potato Pathogen Phytophthora infestans Share Homology with Human Mucins." Molecular Plant-Microbe Interactions® 13, no. 1 (January 2000): 32–42. http://dx.doi.org/10.1094/mpmi.2000.13.1.32.

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We have cloned genes of Phytophthora infestans, the causal agent of potato late blight, that are activated shortly before the onset of invasion of the host tissue. The three genes isolated appear to be arranged in a genomic cluster and belong to a small polymorphic gene family. A conspicuous feature of the deduced proteins is an internal octapeptide repeat with the consensus sequence TTYAP TEE. Because of this structural motif, these novel P. infestans proteins were named Car (cyst-germination-specific acidic repeat) proteins. One of the genes, car90, codes for 1,489 amino acids including 120 octapeptide tandem repeats. Car proteins are transiently expressed during germination of cysts and formation of appressoria and are localized at the surface of germlings. The structural motif of tandemly repeated oligopeptides also occurs in a prominent class of proteins, the mucins, from mammals. The P. infestans Car proteins share 51% sequence homology with the tandem repeat region of a subfamily of human mucins. According to the physiological functions ascribed to mucins, we suggest that Car proteins may serve as a mucous cover protecting the germling from desiccation, physical damage, and adverse effects of the plant defense response and may assist in adhesion to the leaf surface.
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Dissertations / Theses on the topic "Acidic oligopeptides"

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Bonnel, Clément. "Oligopeptides construits autour du γ-aminoacide ATC : synthèses, analyses structurales et évaluation biologique." Thesis, Montpellier, 2016. http://www.theses.fr/2016MONTT201.

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Les travaux décrits dans ce manuscrit concernent la synthèse, l’étude structurale et l’évaluation biologique d’oligopeptides abiotiques incorporant le gamma-aminoacide hétérocyclique nommé ATC (acide-4-Aminométhyl-1,3-Thiazole-5-Carboxylique). Les ATCs sont construits autour d’un noyau thiazole et présentent deux points de diversité structurale. De précédents travaux ont déterminé que la présence du noyau thiazole entre les positions alpha et béta bloquait l'angle zéta autour de 0°, structurant les homo-oligomères de poly-(S)-ATCs en une hélice 9 droite et les faisant ainsi entrer dans le domaine des foldamères. Dans une première partie, nous avons entrepris de développer une voie de synthèse simple, flexible et énantiosélective permettant d’obtenir les ATCs stéréochimiquement purs sur une échelle de plusieurs grammes à partir d'alpha-aminoacides commerciaux. L’introduction de la diversité chimique est réalisée via deux étapes-clés que sont la condensation croisée de Claisen et la réaction de cyclisation de Hantzsch. Puis l’identification des marqueurs de structuration RMN et IR-TF des oligomères d'ATCs a été mise à profit pour caractériser le repliement d’hétéro-oligomères combinant ATCs et alpha-aminoacides. Ainsi, une étude structurale par RMN, IR-TF, cristallographie RX et dichroïsme circulaire a démontré que l’enchaînement 1:1 (L)-alpha:(S)-ATC se structurait en un ruban, stabilisé par un réseau intramoléculaire de liaisons hydrogène bifides formant des pseudocycles à 9 et 12 chaînons. La distribution des chaînes latérales le long du squelette principal présente une forte analogie avec l’hélice alpha, ce qui pourrait constituer un atout majeur pour le développement de composés à finalité thérapeutique. La dernière partie de ce travail a porté sur la conception de pseudo-peptides amphipatiques pour des applications en temps qu'antimicrobiens
This manuscript describes the synthesis, the structural study and the biological evaluation of abiotic oligopeptides incorporating the heterocyclic gamma-amino acid ATC (4-Aminomethyl-1,3-Thiazole-5 Carboxylic acid). This original block is built around a thiazole ring and displays two lateral chains. Previous work in our laboratory highlighted that the presence of the thiazole ring between the positions alpha and beta implied that zeta angle was blocked around 0°, thus structuring poly-(S)-ATCs homo-oligomers in a right-handed 9-helix foldamer. First, development of a simple, flexible and enantioselective synthesis on a few grams scale has allowed to get access of a highly diverse ATC library from commercial alpha-amino acids. Introduction of the chemical diversity occurs via two key steps implying a cross-Claisen condensation and a Hantzsch cyclization. Then identification of NMR and FT-IR structural markers of ATC-containing oligomers was used to characterize the folding propensity of hybrid α:ATC oligomers. We demonstrated that 1:1 (L)-alpha:(S)-ATC heterochiral oligomers are structured in solution in a new ribbon-like shape stabilized by a bidentate intramolecular hydrogen bond network forming 9- and 12-membered pseudorings. The distribution of lateral chains along the main skeleton shows a high analogy with alpha-helix thus constituting a major advantage for potential medicinal applications. The last part of this work has focused on the design of amphipathic ATC-containing pseudo-peptides as antimicrobial agents
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Sawhney, Ashish. "Synthesis and mass spectrometry studies of oligopeptides." Scholarly Commons, 2012. https://scholarlycommons.pacific.edu/uop_etds/831.

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This thesis discusses two major projects. The first project focuses on understanding the effect of chirality on intrinsic acidity of oligopeptides. Gas-phase acidity (ΔacidG) and related thermochemical parameters (ΔacidH, and ΔacidS), of model N- and C-terminal cysteine polyalanine peptides in which one L-alanine was substituted by a D-alanine viz. CAADA and AADAC, were measured by the extended Cooks kinetic method. Gas-phase acidities of CAADA and AADAC were measured to be about 318 kcal/mol and 322 kcal/mol, respectively. These values are different from the gas-phase acidities of the all L-amino acid containing analogues of the above peptides, but suggest that D-alanine containing peptides show the same trend as their all L-amino acid analogues with the N-terminal cysteine peptide being more acidic than the C-terminal cysteine peptide. However, the difference in the acidities of CAADA and AADAC is about 4 kcal/mol which is about half of the difference between their all L-amino acid analogues. These results also suggest that, presumably, a single L-alanine to D-alanine substitution has a moderate effect on the conformation of the respective peptides. The aim of the second project is to understand how acidic amino acids influence peptide fragmentation during tandem mass spectrometric analysis. A series of model N- and C- terminal glutamic acid polyalanine and polyglycine (EAn, AnE (n=2,3); EGn (n=2,3), GnE (n=2-4)) and cysteine polyalanine (CAn, AnC (n=4-6)) peptides were studied. Primarily, EAn and EGn peptides formed bn ions. In contrast, while EOn peptides formed all yn ions, EAn peptides formed fewer yn ions. Similarly, AnE and GnE peptides also formed bn ions. No major differences were observed in yn ion formation. For both sets of peptides, water loss seemed to trend with the position of glutamic acid. CAn and AnC peptides also formed bn ions, just like their glutamic acid counterparts. However, yn ions were observed only for AnC peptides. For all sets of peptides, ions related to bn and yn ions were also observed.
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Kapota, Catherine. "Interactions du cation sodium avec des molécules d'intérêt biologique : acides aminés et oligopeptides." Phd thesis, Ecole Polytechnique X, 2005. http://pastel.archives-ouvertes.fr/pastel-00001365.

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Il existe, aujourd'hui, de nombreuses et efficaces méthodes de caractérisation structurale tridimensionnelle de composés biologiques en phase condensée (RMN, diffraction des rayons X ou dichroïsme circulaire). Depuis une dizaine d'années, ce champ d'études s'est étendu à la phase gazeuse. Ce travail s'inscrit dans ce contexte et concerne le rôle structurant de Na+ sur les acides aminés Gly et Pro et sur des oligo-peptides de Gly et Ala, en combinant approches théoriques et expérimentales de spectroscopie infrarouge d'ions gazeux par dissociation multiphotonique (IRMPD) couplée à la spectrométrie de masse. Les spectres IRMPD expérimentaux des complexes sodiés d'acide aminé, nous ont permis d'identifier la présence exclusive de la forme zwitterionique dans le cas de Pro-Na+ et la présence de la forme non-zwitterionique dans le cas de Gly-Na+, conformément aux résultats de chimie quantique. Ainsi nous avons fourni la première démonstration directe de la présence d'un zwitterion d'acide aminé en phase gazeuse. Il s'agissait des premiers spectres infrarouge d'ions biologiques en phase gazeuse. L'étude théorique des complexes Glyn-Na+ et Alan-Na+ a montré que, pour n<=5, les conformères de plus basse énergie maximisent l'interaction électrostatique du métal avec les n groupements carbonyles, avec ou sans l'amine terminale. Ce comportement a été confirmé d'une part, par des expériences de spectroscopie IRMPD pour n=2,3 et d'autre part, par la détermination des énergies de liaison de ces complexes par la méthode cinétique de Cooks (n=2-4). Pour l'étude théorique de Glyn-Na+, 5<=n<=10, nous avons couplé des recherches conformationnelles Monte-Carlo basées sur des calculs de champ de forces AMBER, à des optimisations par calculs de type ri-BLYP utilisant l'approximation "résolution de l'identité". Cette approche a permis d'explorer en détail des sur! faces de potentiel très complexes. On peut distinguer deux classes limites de conformères, celle où le peptide est globulaire et celle où il adopte une conformation en hélice alpha ou 310. Nous avons montré que les structures les plus basses en énergie présentent le plus souvent une complexation tétradentate avec une forte auto-solvatation. Ces structures sont toutes globulaires pour n<10. Dans le cas de Gly10-Na+, le conformère le plus bas en énergie a une structure globulaire autour du sodium et un domaine de cinq résidus en hélice 310.
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Shen, Jialin. "The variation of the gas phase acidity of a cysteine residue in oligopeptides." Scholarly Commons, 2011. https://scholarlycommons.pacific.edu/uop_etds/791.

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The altered acidities of amino acid residues in folded proteins can be used as a good indication for the diverse functions, stabilities as well as folding-unfolding states of the proteins. Previously, our group has investigated the gas phase acidities of a series of cysteine containing peptides of four residues and longer. The results showed that the helix macrodipole might have a significant influence on the acidities of these peptides. In this work, the gas phase acidities of isomeric small cysteine containing di- and tri-peptides were investigated experimentally and computationally. The gas phase acidities (ΔacidG) and related thermochemical quantities (ΔacidH and ΔacidS) were determined by using the extended Cooks kinetic method. A triple-quadruple mass spectrometer interfaced with an electrospray ionization source was employed for the study. The gas phase acidities of the N-terminal cysteine peptides (CysAla1,2NH2 and CysGly1,2NH2) were determined to be in the range of 321-323 kcal/mol, and the acidities of the C-terminal cysteine peptides (Ala1,2CysNH2 and Gly1,2CysNH2) were around 327- 331 kcal/mol. The results showed that theN-cysteine peptides were more acidic than the corresponding C-cysteine peptides, tri-peptides were stronger acids than di-peptides, and the acidities of cysteine-polyglycine peptides were close to those of the cysteine-polyalanine analogues. Computational studies were performed through conformer search, geometry optimization, and energy calculations using the Spartan and the Gaussian suite of programs. The results showed that the low energy conformations of all deprotonated peptides were coils. The greater acidities of the N-cysteine peptides were likely due to the stronger hydrogen-bonding interactions in the deprotonated N-cysteine peptides, which efficiently stabilized the thiolate anions. The theoretically predicted acidities were in good agreements with the experimental results.
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Breitenkamp, Rebecca Boudreaux. "Oligopeptide-functionalized Graft Copolymers: Synthesis and Applications in Nucleic Acid Delivery." Amherst, Mass. : University of Massachusetts Amherst, 2009. http://scholarworks.umass.edu/open_access_dissertations/5/.

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Akamatsu, Miki. "Quantitative Analysis of Hydrophobicity of Oligopeptides Using Physicochemical Amino Acid Side Chain Parameters and Submolecular Structural Descriptors." Kyoto University, 1990. http://hdl.handle.net/2433/78240.

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Dale, Ryan K. "Temperature and the biological response a multivariate statistical analysis of the variation in genomic organization, oligopeptide frequencies, and environmental temperature /." Access to citation, abstract and download form provided by ProQuest Information and Learning Company; downloadable PDF file, 235 p, 2009. http://proquest.umi.com/pqdweb?did=1654488371&sid=7&Fmt=2&clientId=8331&RQT=309&VName=PQD.

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Barbot, Laurence. "Etude de l'expression intestinale de transporteurs d'acides aminés et d'oligopeptides au cours de la cryptosporidiose expérimentale chez le raton non sevré." Paris 5, 2002. http://www.theses.fr/2002PA05P617.

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Cryptosporidium parvum, parasite de l'épithélium intestinal, est reconnu comme une cause majeure de diarrhée chez les jeunes enfants à l'origine d'une malnutrition et d'un retard de croissance. Afin d'explorer les mécanismes de cette malnutrution, nous avons étudié l'expression intestinale de transporteurs d'acides aminés, EAAT3 et NBAT, et d'oligopeptides PEPT1, au cours de l'infection dans un modèle de crytosporidiose aigue͏̈ chez le raton âgé de 4 à 50 jours. Nous montrons que l'implantation du parasite induit au pic de l'infection une dérégulation respectivement négative et positive de l'expression de EAAT3 et de PEPT1 tout le long de l'intestin grêle. Ces dérégulations impliquent des mécanismes transcriptionnels et post-traductionnels liés d'une part à l'implantation du parasite, et d'autre part à l'hypophagie et à la réponse immunitaire muqueuse. Ces résultats mettent en avant l'intérêt d'une prise en charge nutritionnelle précoce et prolongée des patients infectés par C. Parvum
Crytosporidium parvum is now recognized as being a major cause of diarrheal disease leading to malnutrition and growth retardation in young children. In order to assess the mechanism of C. Parvum-induced malnutrution, we investigated the intestinal expression of animo acid (EAAT3 and NBAT) and oligopeptides (PEPT1) transporters in an acute model of cryptosporidiosis in suckling rat aged from 4 to 50 days. We shown that parasite development induces a down- and up-regulation of PEPT1 and EAAT3 expression respectively along the entire small intestine at the peak of infection. Both transcriptional and post-translational mechanisms are involved in response to parasite implantation, hypophagia and mucosal immune response. .
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Marini, Joseph Thomas. "Development and implementation of a FT-ICR mass spectrometer for the investigation of ion conformations of peptide sequence isomers containing basic amino acid residues by gas-phase hydrogen/deuterium exchange." Diss., Texas A&M University, 2003. http://hdl.handle.net/1969.1/115.

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The gas-phase hydrogen/deuterium (H/D) exchange of protonated di- and tripeptides containing a basic amino acid residue has been studied with a Fourier transform ion cyclotron resonance (FT-ICR) mass spectrometer. Bimolecular reactions are monitored as a function of time providing exchange efficiencies and temporal distributions for the peptide ions. Results from these experiments indicated that position of the basic residue within the peptide (i.e. N-terminal, internal, or C-terminal) influences gas-phase H/D exchange, suggesting unique peptide ion conformations. The FT-ICR mass spectrometer employed for these gas-phase H/D exchange studies was modified from its original design. Instrument modifications include development of an internal matrix assisted laser desorption ionization (MALDI) source for peptide protonation. In addition, a two-section cell was utilized, allowing control of ion motion and factors affecting gas-phase ion molecule reactions. Systems investigated in these gas-phase H/D exchange studies are peptides containing the same amino acid residues but different sequences. These sequence isomers display dissimilar reaction efficiencies and temporal distributions for deuterium incorporation depending on the primary structure of the peptide ion. Specifically, [M+H]+ peptide ions containing a N-terminal basic residue demonstrate unique H/D exchange behavior when compared to their internal and C-terminal counterparts. These differences are attributed to dissimilar intramolecular bridging interactions involved with inductive stabilization of the charge site. Gas-phase H/D exchange of peptide sequence isomers was also probed with various deuterium reagents. Findings suggest that different reagents also influence H/D exchange reaction rate efficiencies and temporal distributions. These dissimilarities are ascribed to relative gas-phase basicity and proposed mechanistic exchange differences for the deuterium reagents.
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Awussi, Ahoefa Ablavi. "Caractérisation génétique et biochimique du système protéolytique de Streptococcus thermophilus : étude de la variabilité des systèmes de transport d’oligopeptides ; caractérisation des phénomènes d’ancrage, de maturation et de libération de la protéase PrtS ; production de peptides bioactifs à partir de caséines bovines." Thesis, Université de Lorraine, 2016. http://www.theses.fr/2016LORR0099/document.

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Nous nous intéressons à la production de peptides bioactifs dans des laits fermentés par la bactérie lactique Streptococcus thermophilus. Pour ce faire, il est nécessaire que cette bactérie en internalise le moins possible lors de sa croissance. Il était donc important de caractériser le système protéolytique S. thermophilus. Tout d’abord, les relations phylogéniques liant 30 souches de S. thermophilus ont été recherchées par MLST. Ensuite, un système de transport de type ABC qui semble fonctionnel a été identifié chez la souche LMD-9 et appelé OTS. Une étude de la variabilité des systèmes de transport Ami et OTS des 30 souches de S. thermophilus a été réalisée. Enfin, l’hydrolyse des caséines par la protéase PrtS de S. thermophilus a été étudiée. Cette protéase habituellement ancrée à la paroi de la bactérie est retrouvée chez la souche 4F44 également sous forme libre. La séquence protéique de PrtS4F44, différente de celle de PrtS de la souche LMD 9 (PrtSLMD-9), n’est pas la cause de la libération partielle de PrtS4F44. La sortase A, acteur de l’ancrage de PrtS à la paroi de la bactérie, présente chez la souche 4F44 (srtA4F44) un allèle différent de celui de la souche LMD-9 (srtALMD-9). En effet, PrtSLMD-9 se trouve libérée lorsque srtALMD-9 est remplacée par srtA4F44 dans la souche LMD-9 montrant ainsi que SrtA4F44 est déficiente, entrainant par conséquent un défaut d’ancrage de PrtS4F44 et sa libération partielle dans le milieu extracellulaire. L’hydrolyse des caséinates bovines totales par la forme libre de PrtS4F44 a permis d’obtenir des peptides bioactifs qui pourront être utilisés pour la fonctionnalisation de produits laitiers fermentés
We are interested in the production of bioactive peptides in fermented milk by the lactic acid bacterium Streptococcus thermophilus. For this, it requires that the bacterium internalize them as few as possible during its growth. Therefore, it was important to characterize the proteolytic system of S. thermophilus. First, phylogenetic relationships linking 30 S. thermophilus strains have been searched by MLST. Secondly, an ABC-type transport system which seems to be functional was identified in the LMD-9 strain and named OTS. A study of the variability of Ami and OTS transport systems of the 30 strains of S. thermophilus was performed. Finally, the hydrolysis of caseins by proteinase PrtS of S. thermophilus was studied. This proteinase usually anchored to the wall of the bacterium was also found in a free form in strain 4F44. The protein sequence of PrtS4F44, different from the one of PrtS in the LMD-9 strain (PrtSLMD-9), is not the cause of the partial release of PrtS4F44. Sortase A, the actor of the anchoring of PrtS to the wall of the bacteria, presents different alleles between the strain 4F44 (srtA4F44) and the LMD-9 strain (srtALMD-9). Indeed, PrtSLMD-9 is released when srtALMD-9 is replaced by srtA4F44 in the strain LMD-9 showing that SrtA4F44 is deficient, causing consequently a default of PrtS4F44 anchoring and its partial release into the extracellular medium. Additionally, hydrolysis of bovine caseinates was performed using the free form PrtS4F44 and allowed the production of bioactive peptides that can be used for the functionalization of fermented dairy products
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Books on the topic "Acidic oligopeptides"

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[Alpha]-aminoacid-N-carboxy-anhydrides and related heterocycles: Syntheses, properties, peptide synthesis, polymerization. Berlin: Springer-Verlag, 1987.

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Book chapters on the topic "Acidic oligopeptides"

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Sapse, Anne-Marie. "Oligopeptides That Are Anticancer Drugs." In Molecular Orbital Calculations for Amino Acids and Peptides, 138–49. Boston, MA: Birkhäuser Boston, 2000. http://dx.doi.org/10.1007/978-1-4612-1354-3_12.

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Kokkinidis, M., D. Tsernoglou, and H. Brückner. "SYNTHESIS AND X-RAY ANALYSIS OF OLIGOPEPTIDES CONTAINING ɑ-AMINOISOBUTYRIC ACID (AIB)." In Porto Carras, Chalkidiki, Greece, Aug. 31–Sept. 5, 1986, edited by Dimitrios Theodoropoulos, 319–22. Berlin, Boston: De Gruyter, 1987. http://dx.doi.org/10.1515/9783110864243-073.

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Kimura, Yukitaka, Motohiro Shima, Tomoyuki Notsu, Shuji Adachi, and Ryuichi Matsuno. "Trypsin-Catalyzed Synthesis of Oligopeptides Containing Hydrophilic and Essential Amino Acid, L-Lysine." In Developments in Food Engineering, 582–84. Boston, MA: Springer US, 1994. http://dx.doi.org/10.1007/978-1-4615-2674-2_187.

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Li, Geng, Alankar Vaidya, Wenchun Xie, Wei Gao, and Richard A. Gross. "Enzyme-Catalyzed Oligopeptide Synthesis: Rapid Regioselective Oligomerization ofL-Glutamic Acid Diethyl Ester Catalyzed by Papain." In ACS Symposium Series, 294–308. Washington, DC: American Chemical Society, 2008. http://dx.doi.org/10.1021/bk-2008-0999.ch020.

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Akamatsu, Miki, Tamio Ueno, and Toshio Fujita. "Applications of a New Hydrophobicity Parameter of Amino Acid Side Chains to Quantitative Structure—Activity Analyses of Oligopeptides." In ACS Symposium Series, 229–39. Washington, DC: American Chemical Society, 1995. http://dx.doi.org/10.1021/bk-1995-0606.ch017.

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Beaumais, J., and Th Ackermann. "L-Phenylalanine Oligopeptides Grafted Poly(Acrylic Acid). Evidence of Specific Interactions of Ethidium Bromide and Acridine Orange with Hydrophobic Microdomains." In Microdomains in Polymer Solutions, 33–49. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4613-2123-1_3.

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Silbernagl, Stefan, and Michael Gekle. "Amino Acids, Oligopeptides, and Hyperaminoacidurias." In Seldin and Giebisch's The Kidney, 2021–44. Elsevier, 2008. http://dx.doi.org/10.1016/b978-012088488-9.50075-9.

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Yildiz, Fatih. "Amino Acids, Oligopeptides, Polypeptides, and Proteins." In Advances in Food Biochemistry, 51–100. CRC Press, 2009. http://dx.doi.org/10.1201/9781420007695-c3.

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"Chapter Amino Acids, Oligopeptides, Polypeptides, and Proteins." In Advances in Food Biochemistry, 65–114. CRC Press, 2009. http://dx.doi.org/10.1201/9781420007695-8.

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Camargo, Simone M. R., Victoria Makrides, Robert Kleta, and François Verrey. "Kidney Transport of Amino Acids and Oligopeptides, and Aminoacidurias." In Seldin and Giebisch's The Kidney, 2405–23. Elsevier, 2013. http://dx.doi.org/10.1016/b978-0-12-381462-3.00071-9.

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Conference papers on the topic "Acidic oligopeptides"

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Niculescu, Mihaela-Doina, Cristina Emanuela Enascuta, Maria Stanca, Carmen Cornelia Gaidau, Cosmin Alexe, Mihai Gidea, and Marius Becheritu. "Complexes based on collagen and keratin for applications in agriculture." In The 8th International Conference on Advanced Materials and Systems. INCDTP - Leather and Footwear Research Institute (ICPI), Bucharest, Romania, 2020. http://dx.doi.org/10.24264/icams-2020.ii.19.

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In the circular economy context, the use of proteins from collagen and keratin by-products of leather industry to obtain products for agriculture serves to reduce the carbon footprint generated from industry by reducing the amount of chemical synthesis products administered in agricultural technologies. This paper presents complexes based on collagen and keratin extracts obtained from by-products of the leather industry and their characterization. Thermal and chemical-enzymatic hydrolysis of semi-processed leather and degreased wool by-products was performed for protein extraction. Complexes were obtained by addition and crosslinking with active principles and vegetable tannins to collagen and keratin extracts. The characterization of complexes was performed based on the results of analytical investigations by physico-chemical methods: volumetry, potentiometry, IR spectroscopy, Dynamic Light Scattering and Texture Analysis. It has been found that collagen and keratin extracts contain sufficient proportions of small and medium size components size, of the order of 1-100 nm and of 100-1000 nm, specific for free amino acids and small oligopeptides with a role in bio stimulating seed germination, but also contain large size components, over 1000 nm, in considerable proportions, which provide the adhesive and film-forming properties, with a role in foliar application and retarded release of amino acids.
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Yamamoto, K., H. Kawasaki, K. Suzuki, K. Tanoue, G. Kosaki, and H. Yamazaki. "AMINO ACID SEQUENCE OF THE THROMBIN-BINDING SITE ON PLATELET GLYCOPROTEIN Ib." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642924.

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Amino acid sequence of the thrombin-binding site on platelet glycoprotein (GP) Ib was determined and the effects of the synthesized analogous peptides on thrombin-induced aggregation were studied. Crude platelet membrane fraction solubilized with 5mM dithiothreitol and 0.2% Tween 20 was applied to a WGA-Sepharose. The bound fractions were eluted with 0.3M N-actylglucosamine, then applied to a TM60 ( a monoclonal antibody against GP Ib)-Affi-gel column. Only one GP was bound to the column and was eluted with 50mM glycine-HCl, pH3.0, containing 0.2% Tween 20. SDS-PAGE showed a single band of 130kDa, corresponding to GP Ib alpha chain (GP Ibα). When the purified GP Ibα was digested with trypsin, two fragments (94kDa . and 43kDa) were obtained. The 43kDa fragment was shown to bind to both affinity colomns of TM60- and thrombin-Affi-gel, while the 94kDa fragment did not bind to either Affi-gel. When the same experiment was performed using chymotrypsin, three fragments (94kDa, 45kDa and 39kDa) were observed. On TM60- and thrombin-Affi-Gel columns, the smaller fragments (45kDa and 39kDa) were bound to both columns. However, on. thrombin-Affi-Gel column, 39kDa fragment was found in both unbound and bound fractions. It showed that the 45kDa fragment interacts with thrombin with a higher affinity than the 39kDa fragment. These results indicate that the thrombin-binding site is located on the "tail" portion of GPIba, especially on a chymotryptic cleavage site.Then 43kDa tryptic fragment was purified and its partial amino acid sequence was analyzed using gas phase amino acid sequence analyzer. Based on its amino acid sequence, several analogous oligopeptides were synthesized. Three peptides (#1-10, #11-23, #17-28) inhibited 0.05 U/ml thrombin-induced aggregations of washed human platelets in dose-dependent manners. IC50 were in the range of L50-550μM for each of these peptides.
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