Relevant bibliographies by topics / Peptides α-D

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  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers

Academic literature on the topic 'Peptides α-D'

Author: Grafiati
Published: 4 June 2021
Last updated: 27 July 2025

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Journal articles on the topic "Peptides α-D"

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Oppegård, Camilla, Per Rogne, Per Eugen Kristiansen, and Jon Nissen-Meyer. "Structure analysis of the two-peptide bacteriocin lactococcin G by introducing d-amino acid residues." Microbiology 156, no. 6 (2010): 1883–89. http://dx.doi.org/10.1099/mic.0.038430-0.

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The importance of 3D structuring in the N- and C-terminal ends of the two peptides (39-mer LcnG-α and 35-mer LcnG-β) that constitute the two-peptide bacteriocin lactococcin G was analysed by replacing residues in the end regions with the corresponding d-isomeric residues. When assayed for antibacterial activity in combination with the complementary wild-type peptide, LcnG-α with four d-residues in its C-terminal region and LcnG-β with four d-residues in either its N- or its C-terminal region were relatively active (two- to 20-fold reduction in activity). 3D structuring of the C-terminal region
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PIMENTA, Daniel C., Iseli L. NANTES, Eduardo S. de SOUZA, et al. "Interaction of heparin with internally quenched fluorogenic peptides derived from heparin-binding consensus sequences, kallistatin and anti-thrombin III." Biochemical Journal 366, no. 2 (2002): 435–46. http://dx.doi.org/10.1042/bj20020023.

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Internally quenched fluorogenic (IQF) peptides bearing the fluorescence donor/acceptor pair o-aminobenzoic acid (Abz)/N-(2,4-dinitrophenyl)ethylenediamine (EDDnp) at N- and C-terminal ends were synthesized containing heparin-binding sites from the human serpins kallistatin and antithrombin, as well as consensus heparin-binding sequences (Cardin clusters). The dissociation constant (Kd), as well as the stoichiometry for the heparin–peptide complexes, was determined directly by measuring the decrease in fluorescence of the peptide solution. Experimental procedures were as sensitive as those used
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Wu, Bo, та Weiping Zheng. "Bis-Lactam Peptide [i, i+4]-Stapling with α-Methylated Thialysines". Molecules 25, № 19 (2020): 4506. http://dx.doi.org/10.3390/molecules25194506.

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Four bis-lactam [i, i+4]-stapled peptides with d- or l-α-methyl-thialysines were constructed on a model peptide sequence derived from p110α[E545K] and subjected to circular dichroism (CD) and proteolytic stability assessment, alongside the corresponding bis-lactam [i, i+4]-stapled peptide with l-thialysine. The % α-helicity values of these four stapled peptides were found to be largely comparable to each other yet greater than that of the stapled peptide with l-thialysine. An l-α-methyl-thialysine-stapled peptide built on a model peptide sequence derived from ribonuclease A (RNase A) was also
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Fox, Robert I., and Ho-Il Kang. "Mechanism of Action of Antimalarial Drugs: Inhibition of Antigen Processing and Presentation." Lupus 2, no. 1_suppl (1993): 9–12. http://dx.doi.org/10.1177/0961203393002001031.

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Recent studies have elucidated the steps involved in the association of antigenic peptides with major histocompatibility complex (MHC) encoded proteins and have suggested how antimalarial compounds might influence this important site of immune activation. These steps of antigen presentation in the macrophage (or other antigen-presenting cells) include: (a) the partial proteolytic degradation of endogenous and exogenous proteins into peptides within the lysosome; (b) the synthesis of MHC class II (i.e. HLA-D associated) α, β, and invariant (Ii) chains in the endoplasmic reticulum; (c) the initi
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Partridge, Anthony W., Hung Yi Kristal Kaan, Yu-Chi Juang, et al. "Incorporation of Putative Helix-Breaking Amino Acids in the Design of Novel Stapled Peptides: Exploring Biophysical and Cellular Permeability Properties." Molecules 24, no. 12 (2019): 2292. http://dx.doi.org/10.3390/molecules24122292.

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Stapled α-helical peptides represent an emerging superclass of macrocyclic molecules with drug-like properties, including high-affinity target binding, protease resistance, and membrane permeability. As a model system for probing the chemical space available for optimizing these properties, we focused on dual Mdm2/MdmX antagonist stapled peptides related to the p53 N-terminus. Specifically, we first generated a library of ATSP-7041 (Chang et al., 2013) analogs iteratively modified by L-Ala and D-amino acids. Single L-Ala substitutions beyond the Mdm2/(X) binding interfacial residues (i.e., Phe
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Torshin, I. Yu, T. E. Bogacheva, and O. A. Gromova. "Placenta peptides: antibacterial effects." Pharmacokinetics and Pharmacodynamics, no. 4 (January 22, 2024): 15–22. http://dx.doi.org/10.37489/2587-7836-2023-4-15-22.

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Mass spectrometric sequencing of peptides in Laennec indicated the presence of 5 peptides in the drug, the biological activity of which may determine the antibacterial properties of the drug. The most significant result of this study is the presence in Laennec of a fragment of the antibacterial peptide cathelicidin (LL-37), an important vitamin D-dependent factor of innate immunity. Other Laennec peptides help reduce excess inflammation by inhibiting the activity of the NF-kB protein, which mediates the effects of TNF-α.
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Hemshekhar, Mahadevappa, Sana Faiyaz, Ka-Yee Grace Choi, Oleg V. Krokhin та Neeloffer Mookherjee. "Immunomodulatory Functions of the Human Cathelicidin LL-37 (aa 13–31)-Derived Peptides are Associated with Predicted α-Helical Propensity and Hydrophobic Index". Biomolecules 9, № 9 (2019): 501. http://dx.doi.org/10.3390/biom9090501.

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The anti-endotoxin activity of the cationic peptide LL-37 and its derivative IG-19 is attributed to electrostatic interaction of the peptides’ positive charge with negatively charged bacterial lipopolysaccharides (LPS), and in part to the alteration of intracellular mechanisms independent of peptide binding to LPS. We examined the immunomodulatory responses induced by IG-19 and four IG-19-derived scrambled peptides (IG-19a–d), in the presence and absence of LPS, in macrophages and peripheral blood-derived mononuclear cells. All peptides had identical net charge (+5) and amino acid composition,
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Kindahl, Lill, Corine Sandström, A. Grey Craig, Thomas Norberg, and Lennart Kenne. "1H NMR studies on the solution conformation of contulakin-G and analogues." Canadian Journal of Chemistry 80, no. 8 (2002): 1022–31. http://dx.doi.org/10.1139/v02-115.

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The conformation of contulakin-G, a bioactive 16 amino acid O-linked glycopeptide (ZSEEGGSNAT*KKPYIL) with the disaccharide β-D-Gal(1[Formula: see text]3)α-D-GalNAc attached to the threonine residue in position 10, has been investigated by 1H NMR spectroscopy. The 1H NMR data for the non-glycosylated peptide and for two glycopeptide analogues, one with the monosaccharide α-D-GalNAc at Thr10 and one with the disaccharide β-D-Gal(1–>3)α-D-GalNAc at Ser7, all of lower bioactivity than contulakin-G, have also been collected. The chemical shifts, NOEs, temperature coefficients of amide protons,
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Hirao, Takashi, Masahide Sato, Akira Shirahata, and Yoshiyuki Kamio. "Covalent Linkage of Polyamines to Peptidoglycan inAnaerovibrio lipolytica." Journal of Bacteriology 182, no. 4 (2000): 1154–57. http://dx.doi.org/10.1128/jb.182.4.1154-1157.2000.

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ABSTRACT Spermidine and cadaverine were found to be constituents of the cell wall peptidoglycan of Anaerovibrio lipolytica, a strictly anaerobic bacterium. The peptidoglycan was degraded with theN-acetylmuramyl-l-alanine amidase and endopeptidase into two peptide fragments, peptide I and peptide II, at a molar ratio of 4:1. Peptides I and II were identified asl-alanine–d-glutamic acid(αcadaverine)γ meso-diaminopimelic acid (DAP)–d-alanine andl-alanine–d-glutamic acid(αspermidine)γ meso-DAP–d-alanine, respectively. The N1-amino group of spermidine was linked to the α-carboxyl group of the d-glu
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Serrano, Griselda N., George G. Zhanel та Frank Schweizer. "Antibacterial Activity of Ultrashort Cationic Lipo-β-Peptides". Antimicrobial Agents and Chemotherapy 53, № 5 (2009): 2215–17. http://dx.doi.org/10.1128/aac.01100-08.

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ABSTRACT Previously reported d,l-lipo-α-peptides and their lipo-β-peptide counterparts (C16-KGGK, C16-KAAK, C16-KKKK, and C12-KLLK) were studied, and the lipo-β-peptides were found to retain antimicrobial activity. Likewise, no significant changes in antimicrobial activity were found upon activity comparisons with d,l-amino acid-based lipopeptides or any l-amino acid lipopeptides. As a defined amphipathic structure is unlikely to form with such short molecules and as similar activities were obtained from all lipopeptides, we suspect that the action of membrane permeation is retained.
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Dissertations / Theses on the topic "Peptides α-D"

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Douat, Céline. "Nouvelle synthèse d' α-amino aldéhydes N-protégés/ incorporation post-synthèse de chaînes lipidiques dans des peptides sur support solide". Montpellier 1, 2001. http://www.theses.fr/2001MON13515.

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La première partie de cette thèse est consacrée à la mise au point d'une nouvelle méthode de synthèse d'a-aminoaldéhydes N-protégés. Les a-aminoaldéhydes interviennent dans la synthèse d'amino acides non naturels et dans la préparation de liaisons peptidiques modifiées. Nous proposons une méthode de formation d'a-aminoaldéhydes N-protégés ( Boc, Z ou Fmoc) par réduction de leurs amides de morpholine correspondants. Cette synthèse donne des résultats similaires, au niveau rendements et pureté optique, à ceux obtenues par la méthode de réduction des amides de Weinreb mais présente un avantage pa
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Flamant-Robin, Céline. "Synthèse asymétrique d' α-acides aminés conformationnellement contraints et de lactames dipeptidiques avec incorporation dans les peptides bioactifs". Paris 11, 2003. http://www.theses.fr/2003PA112038.

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Les peptides jouent un rôle primordial dans divers systèmes biologiques en tant qu'hormones, neurotransmetteurs et neuromodulateurs. . . Ce qui leur confère un intérêt considérable. Néanmoins, certaines caractéristiques intrinsèques empêchent leur développement en médicaments. Certains de ces inconvénients peuvent être évités dans les composés peptidomimétiques. Ces composés peuvent être obtenus par l'introduction de contraintes conformationnelles dans les peptides bioactifs. Beaucoup de peptides bioactifs prennent la conformation en coude qui joue un rôle important dans la reconnaissance du r
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Claro, Bárbara Maria Amaro Gonçalves Moedas. "Characterization of the Self-Assembling of antimicrobial D,L- α Cyclic Peptides at Bacterial Model Membranes". Doctoral thesis, 2021. https://hdl.handle.net/10216/136745.

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Vutla, Suresh. "Azacyclopeptide synthesis and their neuroprotective activity against Aβ toxicity". Thesis, 2018. http://hdl.handle.net/1866/25035.

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Le mauvais repliement et l’agrégation des protéines représentent une cause fondamentale des pathologies amyloïdes. Des dépôts de protéines sous la forme de fibrilles amyloïdes sont une composante caractéristique de plus de vingt maladies neurodégénératives incluant la maladie d’Alzheimer, la maladie de Parkinson et la maladie d’Huntington. Des nanotubes composés de peptides-α -D,L cycliques synthétiques peuvent mimer les propriétés structurelles et biochimiques des protéines amyloïdes. L’introduction de résidus aza-aminés dans des peptides α -D,L cycliques a été étudiée dans le but d’augmenter
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Zorn, Chiara [Verfasser]. "Synthesis and structural investigations of α-peptides [alpha-peptides] containing β-aminocyclopropane [beta-aminocyclopropane] dicarboxylic acids / vorgelegt von Chiara Zorn". 2002. http://d-nb.info/965506843/34.

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De, Pol Silvia [Verfasser]. "Synthesis, conformational investigations and applications of α-peptides [alpha-peptides] containing cis-β-aminocyclopropane [cis-beta-aminocyclopropane] dicarboxylic acids / vorgelegt von Silvia De Pol". 2007. http://d-nb.info/983860238/34.

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Book chapters on the topic "Peptides α-D"

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Beaulieu, Pierre L., and Peter W. Schiller. "Chiral synthesis of D-α, ω-diaminoalkanoic acids." In Peptides. Springer Netherlands, 1988. http://dx.doi.org/10.1007/978-94-010-9595-2_50.

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Ledvina, Miroslav, Jan Ježek, David Šaman, Tomáš Vaisar, and Věra Hříbalová. "Lipophilic disaccharide analogs of MDP: Synthesis of O-(2-acetamido-2-deoxy-6-O-acyl-β-D-glucopyranosyl)-(l→4)-N- acetylnormuramoyl-L-α-aminobutanoyl-D-isoglutamine." In Peptides 1992. Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-011-1470-7_153.

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Krause, E., M. Beyermann, M. Dathe, S. Rothemund, G. Krause, and M. Bienert. "Location of amphipathic α-helical domain in CRF using HPLC retention data of double D-amino acid replacement set." In Peptides 1994. Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-1468-4_189.

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Ledvina, M., and J. Jezek. "An alternative synthesis of O-(2-acylamino-2-deoxy-β-D-glucopyranosyl)-(1->4)-N-acetylnormuramoyl-L-α- aminobutanoyl-D-isoglutamines, analogs of GMDP with immunopotentiative activity." In Peptides 1994. Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-1468-4_337.

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Bajusz, S., E. Barabás, I. Fauszt, et al. "Active site-directed thrombin inhibitors: α-Hydroxy-acyl-prolyl-arginals: New orally active stable analogues of D-Phe-Pro-Arg-H." In Peptides 1994. Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-1468-4_152.

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Kim, Do-Hyung, Kyu-Hwan Park, and Kyou-Hoon Han. "Solution Conformation of an α-Conotoxin GI with a D-Tyr at Position 11." In Peptides: The Wave of the Future. Springer Netherlands, 2001. http://dx.doi.org/10.1007/978-94-010-0464-0_224.

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Chen, Yuxin, Colin T. Mant, and Robert S. Hodges. "The Determination of Helix Stability Coefficients Using D-Amino Acid Substitutions in the non-Polar Face of an Amphipathic α-Helical Model Peptide." In Peptides: The Wave of the Future. Springer Netherlands, 2001. http://dx.doi.org/10.1007/978-94-010-0464-0_162.

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Cortez-Díaz, María Dámaris, Fanny d’Orlyé, and Anne Varenne. "Characterization of New Cyclic d,l-α-Alternate Amino Acid Peptides by Capillary Electrophoresis Coupled to Electrospray Ionization Mass Spectrometry." In Methods in Molecular Biology. Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-8793-1_27.

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"Peptide Natural Products I: RiPPs." In Natural Product Biosynthesis. The Royal Society of Chemistry, 2022. http://dx.doi.org/10.1039/bk9781839165641-00100.

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Peptide-based natural products gain stability towards hydrolysis by amidases and peptidases when morphed into frameworks that resist rapid breakdown. There are two major modes of turning the hydrolytically susceptible amide linkages into stable scaffolds: (1) posttranslational modifications of ribosomally released protein precursors or (2) products from nonribosomal protein synthetase (NRPS) assembly lines. This chapter deals with the first, ribosomally-derived peptide precursors, known as RiPPs: ribosomal posttranslationally modified peptides. More than two dozen RiPP-directed, modified stabl
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Kihlberg, Jan. "Glycopeptide synthesis." In Fmoc Solid Phase Peptide Synthesis. Oxford University Press, 1999. http://dx.doi.org/10.1093/oso/9780199637256.003.0012.

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Most eukaryotic proteins, some bacterial and many viral proteins carry structurally diverse carbohydrates that are covalently attached through N- or O-glycosidic bonds to the side chains of asparagine, serine, threonine, hydroxylysine, tyrosine, and hydroxyproline. In nature, N-linked glycoproteins are assembled by post-translational, enzymatic attachment of a common oligosaccharide having the composition Glc3Man9GlcNAc2 to the side chain of asparagine. This saccharide is then modified enzymatically, thereby giving structural variation to the part remote from the protein. However, N-linked gly
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Conference papers on the topic "Peptides α-D"

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Al-Sayah, M., та M. R. Ghadiri. "Anti-Bacterial Self-Assembled Nanotubes of Cyclic D, L-α-Peptides". У NANOTECHNOLOGY AND ITS APPLICATIONS: First Sharjah International Conference on Nanotechnology and Its Applications. AIP, 2007. http://dx.doi.org/10.1063/1.2776714.

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Chemerovski, Marina, Michal Richamn, Sarah Wilk та Shai Rahimipour. "Self-Assembled Cyclic D,L-α-Peptide Architectures with Potent Anti-Amyloidogenic Activity". У The Twenty-Third American and the Sixth International Peptide Symposium. Prompt Scientific Publishing, 2013. http://dx.doi.org/10.17952/23aps.2013.024.

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Bacon-Baguley, Theresa, Suzanne Kendra-Franczak та Daniel Walz. "THROMBOSPONDIN SPECIFICALLY INTERACTS WITH AMINO ACID SEQUENCES WITHIN THE A α- AND B β- CHAINS OF FIBRINOGEN". У XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643822.

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Thrombospondin (TSP) is responsible for the secretion-dependent phase of platelet aggregation. The mechanism of this action is believed to be through the binding of TSP to fibrinogen, resulting in the stabilization of the platelet aggregate. It has been established that the binding of fibrinogen to the platelet surface is dependent upon peptide sequences present, respectively, in the Aa- and y-chains. We have hypothesized that the binding of TSP to fibrinogen is also dependent upon unique fibrinogen peptide sequences. To test this hypothesis we have examined the interaction of TSP and f.ih.r.i
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Schrumpf, Jasmijn, Renate Verhoosel та Pieter Hiemstra. "Vitamin D-mediated expression of the antimicrobial peptide hCAP18/LL-37 and killing of non-typeablehaemophilus influenzae(NTHi) is reduced after 14 days exposure to TNF-α and IL-1β in primary bronchial epithelial cells (PBEC)". У Annual Congress 2015. European Respiratory Society, 2015. http://dx.doi.org/10.1183/13993003.congress-2015.oa1785.

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