Search results for "Peptide bond"

showing 10 items of 45 documents

N-Acyl-glutarimides: Effect of Glutarimide Ring on the Structures of Fully Perpendicular Twisted Amides and N–C Bond Cross-Coupling

2020

N-Acyl-glutarimides have emerged as the most reactive precursors for N-C(O) bond cross-coupling reactions to date, wherein the reactivity is driven by ground-state destabilization of the amide bond. Herein, we report a full study on the effect of a glutarimide ring on the structures, electronic properties, and reactivity of fully perpendicular N-acyl-glutarimide amides. Most notably, this report demonstrates the generality of deploying N-acyl-glutarimides to achieve full twist of the acyclic amide bond, and results in the discovery of N-acyl-glutarimide amide with an almost perfect twist value, τ = 89.1°. X-ray structures of five new N-acyl-glutarimides are reported. Reactivity studies in t…

010405 organic chemistryOrganic ChemistryGlutarimide010402 general chemistryRing (chemistry)01 natural sciences0104 chemical sciencesCrystallographychemistry.chemical_compoundchemistryAmideReagentPerpendicularPeptide bondReactivity (chemistry)TwistThe Journal of Organic Chemistry
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Further synthetic and structural investigations of new pre-organized picket porphyrins

2005

The straightforward synthesis of three new picket porphyrins with a restrained conformation is described. These porphyrins have an unusual behavior due to the conjugated but still flexible nature of their pickets. The crystal structure of their common precusor is also reported and confirms the presumed geometry of this type of picket. Indeed, the latter one is formally obtained by the conjugation of two aromatic rings through an amide bond. Although the specific shape of the picket is expected to overcrowd the center of the porphyrin, it is shown that different types of nucleophilic reagents can add easily on these pickets.

010405 organic chemistryStereochemistryAromaticityGeneral ChemistryConjugated system010402 general chemistry01 natural sciencesPorphyrin[ CHIM ] Chemical Sciences0104 chemical scienceschemistry.chemical_compoundCrystallographychemistryNucleophile[CHIM] Chemical SciencesPeptide bond[CHIM]Chemical SciencesPicketingComputingMilieux_MISCELLANEOUS
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Phosphinotripeptidic Inhibitors of Leucylaminopeptidases

2021

Phosphinate pseudopeptide are analogs of peptides containing phosphinate moiety in a place of the amide bond. Due to this, the organophosphorus fragment resembles the tetrahedral transition state of the amide bond hydrolysis. Additionally, it is also capable of coordinating metal ions, for example, zinc or magnesium ions. These two properties of phosphinate pseudopeptides make them an ideal candidate for metal-related protease inhibitors. This research investigates the influence of additional residue in the P2 position on the inhibitory properties of phosphinopeptides. The synthetic strategy is proposed, based on retrosynthetic analysis. The N-C-P bond formation in the desired compounds is …

0106 biological sciences0301 basic medicineModels MolecularMolecular modelQH301-705.5StereochemistryPhosphinesProtein ConformationSwineLAP inhibitorsligand-enzyme interactionPhosphinate01 natural sciencesAminopeptidaseCatalysisArticleInorganic Chemistry03 medical and health sciencesResidue (chemistry)phosphinate pseudopeptideLeucyl AminopeptidaseMoietyPeptide bondAnimalsBiology (General)Physical and Theoretical ChemistryEnzyme InhibitorsQD1-999Molecular BiologyMagnesium ionmolecular modeling; LAP inhibitors; barley aminopeptidase inhibitor; phosphinate pseudopeptide; ligand-enzyme interaction; organophosphorus compoundSpectroscopyChemistrymolecular modelingOrganic ChemistryGeneral Medicineorganophosphorus compoundPeptide FragmentsComputer Science ApplicationsChemistry030104 developmental biologybarley aminopeptidase inhibitorHordeum vulgare010606 plant biology & botanyInternational Journal of Molecular Sciences; Volume 22; Issue 10; Pages: 5090
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Chromophore-Protein Interplay During the Phytochrome Photocycle Revealed by Step-Scan FTIR Spectroscopy

2018

Phytochrome proteins regulate many photoresponses of plants and microorganisms. Light absorption causes isomerization of the biliverdin chromophore, which triggers a series of structural changes to activate the signaling domains of the protein. However, the structural changes are elusive, and therefore the molecular mechanism of signal transduction remains poorly understood. Here, we apply two-color step-scan infrared spectroscopy to the bacteriophytochrome from Deinococcus radiodurans. We show by recordings in H2O and D2O that the hydrogen bonds to the biliverdin D-ring carbonyl become disordered in the first intermediate (Lumi-R) forming a dynamic microenvironment, then completely detach …

0301 basic medicineInfrared spectroscopyMolecular Dynamics SimulationBiochemistryCatalysis03 medical and health scienceschemistry.chemical_compoundchromophore-protein interplayColloid and Surface ChemistryBacterial ProteinsSpectroscopy Fourier Transform InfraredPeptide bondta116BiliverdinbiologyPhytochromeHydrogen bondBiliverdineta1182WaterHydrogen BondingDeinococcus radioduransGeneral ChemistryChromophorePhotochemical Processesbiology.organism_classification030104 developmental biologychemistryBiophysicsProtein Conformation beta-StrandDeinococcusPhytochromevalokemiaproteiinitSignal transductionstep-scan FTIR spectroscopyAdenylyl CyclasesJournal of the American Chemical Society
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Handling Metalloproteinases.

2016

Substrate cleavage by metalloproteinases involves nucleophilic attack on the scissile peptide bond by a water molecule that is polarized by a catalytic metal, usually a zinc ion, and a general base, usually the carboxyl group of a glutamic acid side chain. The zinc ion is most often complexed by imidazole nitrogens of histidine side chains. This arrangement suggests that the physiological pH optimum of most metalloproteinases is in the neutral range. In addition to their catalytic metal ion, many metalloproteinases contain additional transition metal or alkaline earth ions, which are structurally important or modulate the catalytic activity. As a consequence, these enzymes are generally sen…

0301 basic medicineMetal ions in aqueous solutionGlutamic AcidMatrix metalloproteinaseHydrogen-Ion ConcentrationBiochemistryCombinatorial chemistryCatalysisMetal03 medical and health scienceschemistry.chemical_compoundZinc030104 developmental biologychemistryStructural Biologyvisual_artvisual_art.visual_art_mediumMetalloproteasesMoleculeImidazolePeptide bondAnimalsHumansAstacinHistidineCurrent protocols in protein scienceLiterature Cited
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Conformational studies into N-methylation of alanine diamide models: A quantitative approach

2006

Abstract A systematic theoretical analysis was performed on N -acetyl- l -alanine N ′-methylamide (Ac- l -Ala-NHMe) and the analogues methylated on the N-terminus (Ac- l -(Me)Ala-NHMe), C-terminus (Ac- l -Ala-NMe 2 ), and both N/C-termini (Ac- l -(Me)Ala-NMe 2 ), to evaluate the influence of methylation of the amide group on the conformational properties of the affected residues. The ϕ , ψ potential energy surfaces were calculated at the B3LYP/6-31+G**//HF/3-21G level of theory with inclusion of the solvent (water) effect (SCRF method). The conformers localised were fully optimised at the B3LYP/6-31+G** in vacuo. The accessible areas of the potential energy surfaces; the number of conformer…

AlanineHydrogen bondStereochemistryCondensed Matter PhysicsBiochemistrySolventchemistry.chemical_compoundchemistryAmidePotential energy surfacePeptide bondMoleculePhysical and Theoretical ChemistryConformational isomerismJournal of Molecular Structure: THEOCHEM
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1,5-Disubstituted 1,2,3-Triazoles as Amide Bond Isosteres Yield Novel Tumor-Targeting Minigastrin Analogs.

2021

[Image: see text] 1,5-Disubstituted 1,2,3-triazoles (1,5-Tz) are considered bioisosteres of cis-amide bonds. However, their use for enhancing the pharmacological properties of peptides or proteins is not yet well established. Aiming to illustrate their utility, we chose the peptide conjugate [Nle(15)]MG11 (DOTA-dGlu-Ala-Tyr-Gly-Trp-Nle-Asp-Phe-NH(2)) as a model compound since it is known that the cholecystokinin-2 receptor (CCK2R) is able to accommodate turn conformations. Analogs of [Nle(15)]MG11 incorporating 1,5-Tz in the backbone were synthesized and radiolabeled with lutetium-177, and their pharmacological properties (cell internalization, receptor binding affinity and specificity, pla…

Biodistribution3-TriazolesStereochemistryPeptidomimeticmedia_common.quotation_subject1201 natural sciencesBiochemistryTurn (biochemistry)Drug Discovery[CHIM]Chemical SciencesPeptide bondInternalizationReceptorCancermedia_commonTumor Targeting[CHIM.ORGA]Chemical Sciences/Organic chemistry010405 organic chemistryChemistry123-Triazoles; Peptidomimetics; Structure−activity relationships; Radiopharmaceuticals; Tumor targeting; CancerStructure-Activity RelationshipsOrganic ChemistryBiological activity0104 chemical sciences010404 medicinal & biomolecular chemistryYield (chemistry)PeptidomimeticsRadiopharmaceuticalsACS medicinal chemistry letters
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How copper ions and membrane environment influence the structure of the human and chicken tandem repeats domain?

2019

Abstract Prion proteins (PrPs) from different species have the enormous ability to anchor copper ions. The N-terminal domain of human prion protein (hPrP) contains four tandem repeats of the –PHGGGWGQ– octapeptide sequence. This octarepeat domain can bind up to four Cu2+ ions. Similarly to hPrP, chicken prion protein (chPrP) is able to interact with Cu2+ through the tandem hexapeptide -HNPGYP- region (residues 53–94). In this work, we focused on the human octapeptide repeat (human Octa4, hPrP60–91) (Ac-PHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQ-NH2) and chicken hexapeptide repeat (chicken Hexa4, chPrP54–77) (Ac-HNPGYPHNPGYPHNPGYPHNPGYP-NH2) prion protein fragments. Due to the fact that PrP is a membr…

Circular dichroism010402 general chemistry01 natural sciencesBiochemistryMicelleInorganic Chemistrychemistry.chemical_compoundMembrane LipidsTandem repeatPeptide bondAnimalsHumansAmino Acid SequenceSodium dodecyl sulfateLipid bilayerMembrane mimicking environmentMicelleschemistry.chemical_classification010405 organic chemistryChemistryCopper ionsSodium Dodecyl SulfateHistidine residues0104 chemical sciencesPrion proteinsMembraneTandem Repeat SequencesBiophysicsPotentiometryThermodynamicsGlycoproteinChickensCopper
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Evaluation of Cyclic Amides as Activating Groups in N-C Bond Cross-Coupling: Discovery of N-Acyl-δ-valerolactams as Effective Twisted Amide Precursor…

2021

The development of efficient methods for facilitating N-C(O) bond activation in amides is an important objective in organic synthesis that permits the manipulation of the traditionally unreactive amide bonds. Herein, we report a comparative evaluation of a series of cyclic amides as activating groups in amide N-C(O) bond cross-coupling. Evaluation of N-acyl-imides, N-acyl-lactams, and N-acyl-oxazolidinones bearing five- and six-membered rings using Pd(II)-NHC and Pd-phosphine systems reveals the relative reactivity order of N-activating groups in Suzuki-Miyaura cross-coupling. The reactivity of activated phenolic esters and thioesters is evaluated for comparison in O-C(O) and S-C(O) cross-c…

Coupling (electronics)chemistry.chemical_compoundChemistryStereochemistryAmideOrganic ChemistryElectrophilePeptide bondReactivity (chemistry)Organic synthesisResonance (chemistry)Coupling reactionJournal of Organic Chemistry
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α,β-Dehydroamino acids in naturally occurring peptides

2014

α,β-Dehydroamino acids are naturally occurring non-coded amino acids, found primarily in peptides. The review focuses on the type of α,β-dehydroamino acids, the structure of dehydropeptides, the source of their origin and bioactivity. Dehydropeptides are isolated primarily from bacteria and less often from fungi, marine invertebrates or even higher plants. They reveal mainly antibiotic, antifungal, antitumour, and phytotoxic activity. More than 60 different structures were classified, which often cover broad families of peptides. 37 different structural units containing the α,β-dehydroamino acid residues were shown including various side chains, Z and E isomers, and main modifications: meth…

Dehydroamino acidsStereochemistryClinical BiochemistryPeptideReview ArticleHeterocyclesBiochemistryMethylationResidue (chemistry)IsomerismDepsipeptidesSide chainPeptide bondAmino AcidsDepsipeptidechemistry.chemical_classificationNatural productsbiologyChemistryDehydropeptidesOrganic ChemistryBiological activitybiology.organism_classificationAmino acidBiochemistryZ/E isomerisationPeptidesBacteriaAmino Acids
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