Search results for "dehydroalanine"

showing 10 items of 26 documents

Addition of thiols to the double bond of dipeptide C-terminal dehydroalanine as a source of new inhibitors of cathepsin C.

2017

Addition of thiols to double bond of glycyl-dehydroalanine and phenyl-dehydroalanine esters provided micromolar inhibitors of cathepsin C. The structure-activity studies indicated that dipeptides containing N-terminal phenylalanine exhibit higher affinity towards the enzyme. A series of C-terminal S-substituted cysteines are responsible for varying interaction with S1 binding pocket of cathepsin C. Depending on diastereomer these compounds most likely act as slowly reacting substrates or competitive inhibitors. This was proved by TLC analysis of the medium in which interaction of methyl (S)-phenylalanyl-(R,S)-(S-adamantyl)cysteinate (7i) with the enzyme was studied. Molecular modeling enabl…

0301 basic medicineModels MolecularDouble bondStereochemistryPhenylalanineCysteine Proteinase InhibitorsBiochemistryCathepsin CCathepsin CSubstrate Specificity03 medical and health scienceschemistry.chemical_compoundStructure-Activity Relationship0302 clinical medicineDehydroalanineMoietyAnimalsSulfhydryl CompoundsBinding sitechemistry.chemical_classificationDipeptideAlanineBinding SitesDehydropeptidesDiastereomerEnzyme inhibitorsGeneral MedicineDipeptidesKinetics030104 developmental biologychemistryThiol addition030220 oncology & carcinogenesisCattleBiochimie
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Thiazole–amino acids: influence of thiazole ring on conformational properties of amino acid residues

2021

Abstract Post-translational modified thiazole–amino acid (Xaa–Tzl) residues have been found in macrocyclic peptides (e.g., thiopeptides and cyanobactins), which mostly inhibit protein synthesis in Gram + bacteria. Conformational study of the series of model compounds containing this structural motif with alanine, dehydroalanine, dehydrobutyrine and dehydrophenylalanine were performed using DFT method in various environments. The solid-state crystal structure conformations of thiazole–amino acid residues retrieved from the Cambridge Structural Database were also analysed. The studied structural units tend to adopt the unique semi-extended β2 conformation; which is stabilised mainly by N–H⋯N…

0301 basic medicineStereochemistryClinical BiochemistryNon-standard amino acidsMolecular ConformationRamachandran map010402 general chemistryRing (chemistry)01 natural sciencesBiochemistryDFT03 medical and health scienceschemistry.chemical_compoundDehydroalanineAmino AcidsStructural motifThiazoleOxazoleAlaninechemistry.chemical_classificationHydrogen bondNon-standard amino AIDSHydrogen bondOrganic ChemistryHydrogen Bonding0104 chemical sciencesAmino acidThiazoles030104 developmental biologyConformational analysischemistryOriginal ArticleThiazolePeptidesAmino Acids
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The infrared and Raman spectra of solid tridehydropeptides : influence of ΔAla and ΔPhe on the spectral profile

2012

Abstract A series of solid tripeptides Boc-Gly-X-Gly-OMe (X = dehydroalanine (ΔAla), dehydrophenylalanine (ΔPhe)) was investigated by Raman scattering and Fourier transform infrared spectra to examine the conformational marker bands of the unsaturated residue. The observed fundamental modes gave us the opportunity to analyze structural features that change due to the substitution of Ala by ΔAla and due to the different spatial arrangement of ΔPhe ( Z and E isomers). In addition, we showed the alteration of the spectral profile when the large size residue (Phe) is introduced into the backbone of the peptide with ΔPhe (in Boc-Gly-Δ (Z) Phe-Phe-OMe). The frequency ranges of interest included t…

ChemistryInfraredDehydrophenylalanineAnalytical chemistryTripeptidedehydrophenylalaninetripeptidesDehydroalanineFourier transform infrared spectrachemistry.chemical_compoundsymbols.namesakeCrystallographyDehydroalanineRaman bandAmideTripeptidessymbolsIRdhydroalanineRaman spectroscopyRamanSpectroscopyRaman scattering
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Conformational analysis of α,β-dehydropeptide models at the HF and DFT levels

2004

Abstract The Ramachandran potential energy surfaces of N-acetyl-α,β-dehydroamino acid N′-monomethylamides Ac-ΔXaa-NHMe (ΔXaa=ΔAla, (Z)-ΔPhe; 1, 2) and N-acetyl-α,β-dehydroamino acid N′,N′-dimethylamides Ac-ΔXaa-NMe2 (ΔXaa=ΔAla, (Z)-ΔPhe, (Z)-ΔAbu; 3–5) were calculated at the HF/6-31G*//HF/3-21G level. The conformers localised were fully optimised at the DFT/B3LYP/6-31+G** level and their relative stabilities were analysed in terms of both π-conjugation and internal hydrogen bonding. The Ac-ΔXaa-NMe2 molecules reveal the low-energy conformer H/F, φ=−41±4°, ψ=128±4°, which is not too easily accessible for common amino acid residues. This conformer is stabilised by the bifurcated N2–CH3 O1 int…

DehydrophenylalanineHydrogen bondStereochemistryIntermolecular forceIntramolecular hydrogen bondingPotential energy surfaceCondensed Matter PhysicsDehydroalanineBiochemistryPotential energyDimethylamideschemistry.chemical_compoundchemistryDehydroalaninePotential energy surfaceMoleculePhysical and Theoretical ChemistryConformational isomerismRamachandran plotJournal of Molecular Structure: THEOCHEM
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Synthesis of Tetrapeptide p‐nitrophenylanilides containing dehydroalanine and dehydrophenylalanine and their influence on cathepsin C activity

2001

Three dehydrotetrapeptides of rationally varying structure were prepared and tested as affectors of cathepsin C. These compounds appeared to be substrates of the enzyme, being equipotent with their classical counterparts. Thus, replacement of amino acid in a short peptide by corresponding dehydroamino acid does not prevent cathepsin C in recognizing dehydropeptide as its substrate. Copyright © 2001 European Peptide Society and John Wiley & Sons, Ltd.

Magnetic Resonance SpectroscopyStereochemistryPhenylalaninePeptideBiochemistryCathepsin CCathepsin Cdipeptidyl-peptidase Ichemistry.chemical_compoundStructural BiologyDehydroalanineDrug DiscoveryAnimalsAnilidesAmino AcidsMolecular BiologyPharmacologyCathepsinchemistry.chemical_classificationAlanineTetrapeptideChemistryOrganic ChemistryProteolytic enzymesdehydroamino acidsGeneral Medicineproteolytic enzymesAmino acidEnzymeModels ChemicalBiochemistryMolecular MedicineCattleOligopeptidesSpleenJournal of Peptide Science
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Conformational investigation of α,β-dehydropeptides. X. Molecular and crystal structure of Ac-ΔAla-NMe2 compared with those of Ac-L-Ala-NMe2, Ac-DL-A…

2002

A series of three homologous dimethyldiamides Ac-DeltaAla-NMe2, Ac-L-Ala-NMe2 and Ac-DL-Ala-NMe2 has been synthesized and the structures of these amides determined from single-crystal X-ray diffraction data. To learn more about the conformational preferences of compounds studied, the fully relaxed (phi-psi) conformational energy maps in vacuo (AM1) of Ac-DeltaAla-NMe2 and Ac-L-Ala-NMe2 were obtained, and the calculated minima reoptimized with the DFT/B3LYP/6-31G** method. The crystal-state results have been compared with the literature data. Ac-DeltaAla-NMe2 and other alpha,beta-dehydroamino acid dimethyldiamides, Ac-DeltaXaa-NMe2 adopt the conservative conformation of the torsion angles ph…

Models Moleculardehydroalanine derivativeProtein ConformationStereochemistryαPeptidedimethylamidesCrystal structureX‐ray crystallographyCrystallography X-RayBiochemistryEndocrinologyProtein structureMoleculeBeta (finance)crystal and molecular structuresalanine derivativesβ‐dehydroamino acidstheoretical calculationschemistry.chemical_classificationAlanineamino acid amidesAmino acidCrystallographydehydropeptideschemistryX-ray crystallographyPeptidesRamachandran plotJOURNAL OF PEPTIDE RESEARCH
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Broad Spectrum Thiopeptide Recognition Specificity of theStreptomyces lividans TipAL Protein and Its Role in Regulating Gene Expression

1999

Microbial metabolites isolated in screening programs for their ability to activate transcription of the tipA promoter (ptipA) in Streptomyces lividans define a class of cyclic thiopeptide antibiotics having dehydroalanine side chains ("tails"). Here we show that such compounds of heterogeneous primary structure (representatives tested: thiostrepton, nosiheptide, berninamycin, promothiocin) are all recognized by TipAS and TipAL, two in-frame translation products of the tipA gene. The N-terminal helix-turn-helix DNA binding motif of TipAL is homologous to the MerR family of transcriptional activators, while the C terminus forms a novel ligand-binding domain. ptipA inducers formed irreversible…

Protein ConformationMolecular Sequence DataMutantBiologyBiochemistryStreptomycesMass SpectrometryThiostreptonchemistry.chemical_compoundProtein structureBacterial ProteinsDehydroalanineAmino Acid SequenceMolecular BiologyRegulation of gene expressionAlanineProtein primary structureGene Expression Regulation BacterialCell Biologybiology.organism_classificationStreptomycesAnti-Bacterial AgentschemistryBiochemistryTrans-ActivatorsPeptidesNosiheptideJournal of Biological Chemistry
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Conformational investigation of alpha,beta-dehydropeptides. VIII. N-acetyl-alpha,beta-dehydroamino acid N'-methylamides: conformation and electron de…

2009

The Fourier transform infrared spectra are analyzed in the regions of Vs(N-H), amide I, amide II and Vs(C alpha = C beta) bands for a series of Ac-delta Xaa-NHMe, where delta Xaa = delta Ala, (Z)-delta Abu, (Z)-delta Leu, (Z)-delta Phe and delta Val, to determine the predominant solution conformation of these alpha,beta-dehydropeptide-related molecules and the electron distribution perturbation in their amide bonds. The measurements were performed in dichloromethane (DCM). To confirm and rationalize the assignments, the spectra of the respective series of saturated Ac-Xaa-NHMe, recorded in DCM, and the spectra of these two series of unsaturated and saturated compounds, recorded in acetonitr…

Protein ConformationαAb initioElectronsBiochemistrychemistry.chemical_compoundEndocrinologyDehydroalanineComputational chemistryAb initio quantum chemistry methodsamidic resonanceAmideSpectroscopy Fourier Transform InfraredMoleculePeptide bondC5 hydrogen bondC5 conformationFourier transform infrared spectroscopyamide bond lengthβ‐dehydroamino acidsHydrogen bondab initio calculationsdehydroalanineAmidesMolecular WeightCrystallographyFTIR spectroscopychemistryPeptidesΔ‐electron conjugationThe journal of peptide research : official journal of the American Peptide Society
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CCDC 1034604: Experimental Crystal Structure Determination

2014

Related Article: P. Lenartowicz, M. Makowski, B. Zarychta, K. Ejsmont|2014|Acta Crystallogr.,Sect.E:Struct.Rep.Online|70|599|doi:10.1107/S1600536814025197

Space GroupCrystallographyCrystal SystemCrystal StructureCell ParametersN-(t-butoxycarbonyl)phenylalanyldehydroalanine isopropyl esterExperimental 3D Coordinates
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CCDC 611080: Experimental Crystal Structure Determination

2007

Related Article: D.Siodlak, A.Macedowska-Capiga, K.Ejsmont, J.Zaleski, B.Rzeszotarska|2007|Z.Kristallogr.|222|297|doi:10.1524/zkri.2007.222.6.297

Space GroupCrystallographyCrystal SystemCrystal StructureN-Acetyl-N-methyl-alphabeta-dehydroalanine N'-methylamideCell ParametersExperimental 3D Coordinates
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