0000000001309687
AUTHOR
Maciej Makowski
showing 43 related works from this author
N-[Glycyl-(Z)-α,β-dehydrophenylalanylglycyl-(Z)-α,β-dehydrophenylalanyl]glycine trifluoroacetate methanol solvate
2007
The molecular conformation of the title dehydropeptide, H+-Gly1–ΔZPhe2–Gly3–ΔZPhe4–Gly5-OH·CF3COO−·CH3OH or C24H26N5O6+·CF3COO−·CH3OH, is characterized by the presence of two intramolecular N—H⋯O hydrogen bonds that stabilize two type III β-turns, at the ΔZPhe2 (ΔZPhe is the Z isomer of the α,β-dehydrophenylalanine residue) and Gly3, and Gly3 and ΔZPhe4 residues. As a result, the pentapeptide adopts a right-handed 310-helical conformation. All peptide units are linked trans to each other.
Two phosphonodehydrotripeptides: Boc0–Gly1–Δ(Z)Phe2–α‐Abu3PO3Me2 and Boc0–Gly1–Δ(Z)Phe2–α‐Nva3PO3Et2
2012
The present paper reports the crystal structures of two short phosphonotripeptides (one in two crystal forms) containing one ΔPhe (dehydrophenylalanine) residue, namely dimethyl (3-{[tert-butoxycarbonylglycyl-α,β-(Z)-dehydrophenylalanyl]amino}propyl)phosphonate, Boc0–Gly1–Δ(Z)Phe2–α-Abu3PO3Me2, C21H32N3O7P, (I), and diethyl (4-{[tert-butoxycarbonylglycyl-α,β-(Z)-dehydrophenylalanyl]amino}butyl)phosphonate, Boc0–Gly1–Δ(Z)Phe2–α-Nva3PO3Et2, as the propan-2-ol monosolvate 0.122-hydrate, C24H38N3O7P·C3H8O·0.122H2O, (II), and the ethanol monosolvate 0.076-hydrate, C24H38N3O7P·C2H6O·0.076H2O, (III). The crystals of (II) and (III) are isomorphous but differ in the type of solvent. The phosphono gr…
Pentapeptides containing two dehydrophenylalanine residues - synthesis, structural studies and evaluation of their activity towards cathepsin C
2008
Synthesis, structural and biological studies of pentapeptides containing two Delta Phe residues (Z and E isomers) in position 2 and 4 in peptide chain were performed. All the investigated peptides adopted bent conformation and majority of them could exist as two different. conformers in solution. Only pentapeptides. containing free N-termini appeared to act as weak inhibitors of cathepsin C with the slow-binding, competitive mechanism of inhibition. free acids being bound slightly better than their methyl esters. Results of Molecular modeling suggested significant difference between peptides, depending of the type of amino acid residue in position 5 in peptide chain. Dehydropeptides contain…
Influence of the position of two dehydro-amino acids residues in the oligopeptide sequence on the binding ability towards Cu(II) ions
2005
Abstract Studies on the binding ability of bis-dehydro-hexa- and pentapeptides have shown that the hexapeptides bind Cu+2 with similar efficacy as pentapeptides. The increase of distance between two dehydro-amino acid residues in the peptide backbone has no impact on the efficacy in metal ion binding. The type of isomeration [(Z) or (E)] has an influence on the coordination of the metal ion only to the first amide nitrogen.
Purification and partial characterization of aminopeptidase from barley (Hordeum vulgare L.) seeds.
2013
Aminopeptidases (EC 3.4.11) are proteolytic enzymes, which hydrolyze one amino acid from N-terminus of peptidic substrates. Inhibitors of plant aminopeptidases can find an application in agriculture as herbicides. Isolation and partial characterization of aminopeptidase from barley (Hordeum vulgare L.) seeds has been described. The enzyme was purified to molecular homogeneity using a six-step purification procedure (precipitation with (NH4)2SO4, followed by chromatography on Sephadex G-25, DEAE-Sepharose, Sephacryl HR 300, Macro-Prep Q and Phenyl-Sepharose HP columns). The enzyme was purified 365-fold with recovery above 18%. The molecular weight of the purified enzyme was determined by SDS…
Binding ability of N-Para-amino-phenylsulfonyl derivatives of amino acids. Potentiometric and spectroscopic studies of Cu(II) complexes
1995
Abstract N-Para-amino-phenylsulfonyl derivatives of amino acids are very effective ligands for Cu(II) ions. Potentiometric and spectroscopic results have shown that Cu(II) ions are able to deprotonate and bind to sulfonamide nitrogen below pH 5 to form stable mono- and bis-[N − , COO − ] chelates. The basicity of sulfonamide nitrogen is lower than peptide amide nitrogen and no distinct anchoring site is necessary to promote the amide nitrogen deprotonation.
Impact of α,β-dehydroamino acid residues on the binding abilities of di-, tri- and tetra-peptides
2000
Insertion of a dehydroamino acid residue into a sequence of di-, tri- or tetra-peptide changed considerably the binding abilities of peptide ligands towards copper(II) ions. Potentiometric and spectroscopic (EPR, UV-VIS and CD) data have shown that the amide nitrogen of the dehydroamino acid residue is more effective in co-ordination than its parent analogue. In the case of the bulky ΔPhe residue also the (Z–E) isomerisation has a critical impact on the co-ordination equilibria in the system studied.
Enhanced β-turn conformational stability of tripeptides containing Δphe in cis over trans configuration
2013
Conformations of three pairs of dehydropeptides with the opposite configuration of the Delta Phe residue, Boc-Gly-Delta(Z/E)Phe-Phe-p-NA (Z- p -NA and E- p -NA), Boc-Gly-Delta(Z/E)Phe-Phe-OMe (Z-OMe and E-OMe), and Boc-Gly-Delta(Z/E)Phe-Phe-OH (Z-OH and E-OH) were compared on the basis of CD and NMR studies in MeOH, TFE, and DMSO. The CD results were used as the additional input data for the NMR-based calculations of the detailed solution conformations of the peptides. It was found that Z- p -NA, E- p -NA, Z-OMe, and Z-OH adopt the beta-turn conformations and E-OMe and E-OH are unordered. There are two overlapping type III beta-turns in Z- p -NA, type II' beta-turn in E- p -NA, and type II …
Comparative Studies on IR, Raman, and Surface Enhanced Raman Scattering Spectroscopy of Dipeptides Containing ΔAla and ΔPhe
2012
Three dipeptides containing dehydroresidues (\DeltaAla, \Delta (Z)Phe, and \Delta (E)Phe) were examined by IR, Raman, and surface-enhanced Raman techniques for the first time. The effect of the size and isomer type of the β -substituent in the dehydroresidue on the conformational structure of the peptide was evaluated by using the analysis of IR and Raman bands. Additionally, SERS spectroscopy provided insight into the adsorption mechanism of these species on the metal surface. SERS spectra were recorded at alkaline pH on the silver sol using visible light excitation. The dehydroresidues studied here strongly influenced the SERS profile of the peptides. The most pronounced SERS signal for a…
Binding abilities of dehydropeptides towards Cu(II) and Ni(II) ions. Impact of Z–E isomerization on metal ion binding
2002
The study on the binding ability of dehydro-tri- and tetrapeptides has shown that the alpha,beta-double bond has a critical effect on the peptide coordination to metal ions. It may affect the binding of the vicinal amide nitrogens by the electronic effect and stabilize the complex due to steric effects. The (Z) isomer is the most effective in stabilizing of the complexes formed. The presence of large side chain in the dehydroamino acid residue may also be critical for the coordination mode in the metallopeptide systems.
Kinetics of photochemical isomerization of TFA-Gly-ZΔPhe into TFA-Gly-EΔPhe
2017
The kinetics of photoisomerization of trifluoroacetyl-(Z)-dehydrophenylalanylglycine into trifluoroacetyl-(E)- dehydrophenylalanylglycine was studied in the hope that light-induced reaction could be useful as a means of preparation of the E-dehydropeptides. The obtained results indicate that if this reaction carried out under irradiation with light of wavelength 360 nm it is practically irreversible and gave nearly quantitatively pure Eisomer Significantly, expected cyclic side-products were not observed in the reaction mixture, thus proving the preparative potential of the elaborated procedure.
N-(tert-butoxycarbonylglycyl-alpha,beta-dehydrophenylalanylglycylphenylalanyl)-4-nitroaniline.
2000
In the crystal structure of the tetrapeptide Boc0–Gly1–ΔPhe2–Gly3–Phe4–p-NA (p-NA is para-nitroaniline), C33H36N6O8, there are two independent molecules differing in conformation in the asymmetric part of the unit cell. All the amino acids in the peptide are linked trans to each other. The torsion angles in the main chain of both molecules are close to the values of the type β-II turn. Two intramolecular and three intermolecular N—H⋯O hydrogen bonds stabilize the conformation of each of the molecules.
Crystal structure of N-(tert-butoxycarbonyl)phenylalanyldehydroalanine isopropyl ester (Boc–Phe–ΔAla–OiPr)
2014
In the crystal structure of the dehydrodipeptide (Boc-Phe-ΔAla-OiPr), the molecule has a trans configuration of the N-methylamide group. Its geometry is different from saturated peptides but is in excellent agreement with other dehydroalanine compounds. In the crystal, an N—H⋯O hydrogen bond links the molecules in a herringbone packing arrangement.
Coordination ability of pentapeptides with two dehydro-amino acid residues inserted into their sequences.
2004
The study on the binding ability of tested ligands have shown that insertion of two dehydro-amino acid residues into peptide sequences makes them more effective in metal ion binding than ligands with one dehydro-amino acid residue. The ligand with two Z(Delta)Phe residue form more stable complexes than his analogues with one Z(Delta)Phe residue. Interesting is this that position of Z(Delta)Phe residue in peptide chain have impact on Cu(II)-complexes formation.
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…
Two pentadehydropeptides with different configurations of the ΔPhe residues
2009
Comparison of the crystal structures of two pentadehydropeptides containing DeltaPhe residues, namely (Z,Z)-N-(tert-butoxycarbonyl)glycyl-alpha,beta-phenylalanylglycyl-alpha,beta-phenylalanylglycine (or Boc(0)-Gly(1)-Delta(Z)Phe(2)-Gly(3)-Delta(Z)Phe(4)-Gly(5)-OH) methanol solvate, C(29)H(33)N(5)O(8) x CH(4)O, (I), and (E,E)-N-(tert-butoxycarbonyl)glycyl-alpha,beta-phenylalanylglycyl-alpha,beta-phenylalanylglycine (or Boc(0)-Gly(1)-Delta(E)Phe(2)-Gly(3)-Delta(E)Phe(4)-Gly(5)-OH), C(29)H(33)N(5)O(8), (II), indicates that the Delta(Z)Phe residue is a more effective inducer of folded structures than the Delta(E)Phe residue. The values of the torsion angles phi and psi show the presence of two …
N-[tert-Butoxycarbonylglycyl-(Z)-α,β-dehydrophenylalanylglycyl-(E)-α,β-dehydrophenylalanylphenylalanyl]-4-nitroaniline ethanol solvate
2005
The alpha,beta-dehydrophenylalanine residues influence the conformation of the title pentapeptide Boc0-Gly1-Delta(Z)Phe2-Gly3-Delta(E)Phe4-L-Phe5-p-NA ethanol solvate, C42H43N7O9.C2H5OH. The first unsaturated phenylalanyl (Delta(Z)Phe2) and the third glycyl (Gly3) residues form a type I beta turn, while the second unsaturated phenylalanyl (Delta(E)Phe4) and the last phenylalanyl (L-Phe5) residues are part of a type II beta turn. All the amino acids in the peptide are linked trans to one another. The crystal structure is stabilized by intra- and intermolecular hydrogen bonds.
Michael additions to double bonds of esters of N-protected (s)-phenylalanyldehydroalanine (X-(s)-Phe-ΔAla-OMe) and its phosphonic acid counterpart (X…
2017
Electrophilic addition of amines, thiols and bromide to the double bonds of model dehydrodipeptides and dehydrophosphonodipeptide was studied. The double bond in these two classes of peptides reacted similarly and gave the same products. These results indicate that dehydropeptides are very good candidates as substrates for modifications of peptide side-chains.
N-p-Amino- and N-p-nitro-phenylsulfonyl derivatives of dipeptides, a new family of ligands for copper(II). Potentiometric and spectroscopic studies
1995
The co-ordination ability of four dipeptide analogues substituted on the N-terminal amino group with p-nitrophenylsulfonyl (nps-Ala-Ala and nps-Ala-His) and p-aminophenylsulfonyl (aps-Ala-Ala and aps-Ala-His) groups was studied by potentiometric and spectroscopic (UV/VIS absorption, CD and EPR) techniques. The N-terminal sulfonyl substituent drastically changes the acidity of the sulfonamide proton making nitrogen very efficient in binding to CuII. The sulfonamide nitrogen having pK between 9 and 11 does not need any anchoring binding group to form complexes with CuII. The para substituent on the phenyl ring (amino or nitro) influences very strongly the acidity of the sulfonamide proton. Th…
Quinazoline antifolate thymidylate synthase inhibitors: replacement of glutamic acid by aminophosphonic acids
2003
The synthesis of six analogues of the potent thymidylate synthase (TS) inhibitor N -[4-[ N -[(3,4-dihydro-2-methyl-4-oxo-6-quinazolinoyl)-methyl]- N -prop-2-ynylamino]benzoyl]- L -glutamic acid 2 is described in which the glutamic acid residue has been replaced by DL -aminophosphonic acids. New antifolates were tested as inhibitors of TS isolated from mouse L1210 leukemic cells as well as inhibitors of growth mouse leukemic L5178Y cells. In general these modifications result in compounds that are considerably less potent than 2 as TS inhibitors with K i 's 0.17-1.10 w M. Very poor solubility in water limited their proper assay of growth cells inhibition.
N‐[tert‐Butoxycarbonylglycyl‐(E)‐α,β‐dehydrophenylalanylglycylglycyl‐(E)‐α,β‐dehydrophenylalanyl]glycine
2006
In the molecule of the title hexapeptide, Boc0–Gly1–ΔEPhe2–Gly3–Gly4–ΔEPhe5–Gly6–OH, C31H36N6O9, there are two overlapping β-turns, one of type II on the ΔEPhe2 (ΔEPhe is isomer E of the α,β-dehydrophenylalanine residue) and Gly3 residues and the second of type III′ on the Gly3 and Gly4 residues. All amino acids in the peptide are linked trans to each other. Three relatively strong intramolecular N—H⋯O hydrogen bonds stabilize the crystal structure. Two of them, of the 4→1 type, are responsible for two β-turns in the peptide.
N‐[tert‐Butoxycarbonylglycyl‐(Z)‐α,β‐dehydrophenylalanylglycyl‐(E)‐α,β‐dehydrophenylalanyl]glycine methyl ester dihydrate
2006
The title pentapeptide, Boc0—Gly1–ΔZPhe2—Gly3–ΔEPhe4—Gly5—OMe, C30H35N5O8·2H2O, adopts the type I β-turn conformation for the ΔZPhe2—Gly3 residues. It is stabilized by a 4\rightarrow1 intramolecular hydrogen bond between the ΔEPhe4 NH and Gly1 CO groups. All the amino acid residues in the pentapeptide sequence are linked trans to each other. The crystal structure is stabilized by intra- and intermolecular hydrogen bonds.
Influence of solvents on conformation of dehydropeptides
2013
Abstract Structural investigations of dehydropeptides containing (Z)-dehydrophenylalanine in solvents characterized by different polarity are discussed. The conformational analysis are based on spectroscopic methods (NMR, CD), molecular modeling techniques and in case of the tripeptide, ab initio methods. The results of temperature experiment indicate, that the only conformation of the investigated hexapeptide 3 is stabilized by intramolecular hydrogen bonds. Depending on the length of the peptide chain, the polarity of solvent influences on arrangement of the side chain of the amino acids or of the main chain of the peptide.
Toward engineering efficient peptidomimetics. Screening conformational landscape of two modified dehydroaminoacids
2013
Effective peptidomimetics should posses structural rigidity and appropriate interaction pattern leading to potential spatial and electronic matching to the target receptor site. Rational design of such small bioactive molecules could push chemical synthesis and molecular modeling toward faster progress in medicinal chemistry. Conformational properties of N-t-butoxycarbonyl-glycine-(E/Z)-dehydrophenylalanine N′,N′-dimethylamides (Boc-Gly-(E/Z)-ΔPhe-NMe2) in chloroform were studied by NMR and IR spectroscopy. The experimental findings were supported by extensive calculations at DFT(B3LYP, M06-2X) and MP2 levels of theory and the β-turn tendency for both isomers of the studied dipeptide were d…
Conformation of dehydropentapeptides containing four achiral amino acid residues - controlling the role of L-valine.
2014
Structural studies of pentapeptides containing an achiral block, built from two dehydroamino acid residues (ΔZPhe and ΔAla) and two glycines, as well as one chiral L-Val residue were performed using NMR spectroscopy. The key role of the L-Val residue in the generation of the secondary structure of peptides is discussed. The obtained results suggest that the strongest influence on the conformation of peptides arises from a valine residue inserted at the C-terminal position. The most ordered conformation was found for peptide Boc-Gly-ΔAla-Gly-ΔZPhe-Val-OMe (3), which adopts a right-handed helical conformation.
Sulphonamide Antifolates Inhibiting Thymidylate Synthase. Synthesis, Enzyme Inhibition and Cytotoxicity
1993
Synthesis and biological evaluation are described of seven new analogues (3-9) of two potent thymidylate synthase inhibitors, 10-propargyl-5,8-dideazafolate (1) and its 2-methyl-2-deamino congener ICI 198583 (2). While the new compunds 3 and 4 were analogues of 1 and 2, respectively, containing a p-aminobenzenesulfonyl residue in place of the p-aminobenzoic acid residue, the remaining 5 new compounds were analogues of 4 with the L-glutamic acid residue replaced by glycine (5), L-valine (6), L-alanine (7), L-phenylglycine (8) or L-norvaline (9). The new analogues were tested as inhibitors of thymidylate synthases isolated from tumour (Ehrlich carcinoma), parasite (Hymenolepis diminuta) and n…
Sulfamide antifolates inhibiting thymidylate synthase: synthesis, enzyme inhibition and cytotoxicity
2002
Synthesis and biological evaluation are described of seven new analogues (3-9) of two potent thymidylate synthase inhibitors, 10-propargyl-5,8-dideazafolate (1) and its 2-methyl-2-deamino congener ICI 198583 (2). While the new compunds 3 and 4 were analogues of 1 and 2, respectively, containing a p-aminobenzenesulfonyl residue in place of the p-aminobenzoic acid residue, the remaining 5 new compounds were analogues of 4 with the L-glutamic acid residue replaced by glycine (5), L-valine (6), L-alanine (7), L-phenylglycine (8) or L-norvaline (9). The new analogues were tested as inhibitors of thymidylate synthases isolated from tumour (Ehrlich carcinoma), parasite (Hymenolepis diminuta) and n…
Impact of the ΔPhe configuration on the Boc-Gly-ΔPhe-NHMe conformation: experiment and theory
2019
Conformational propensities of N-t-butoxycarbonyl-glycine-(E/Z)-dehydrophenylalanine N′-methylamides (Boc-Gly-(E/Z)-ΔPhe-NHMe) in chloroform were investigated by NMR and IR techniques. The low-temperature crystal structure of the E isomer was determined by single crystal X-ray diffraction and the experimental data were elaborated by theoretical calculations using DFT (B3LYP, M06-2X) and MP2 approaches. The β-turn tendencies for both isomers were determined in the gas phase and in the presence of solvent. The obtained results reveal that the configuration of ΔPhe residue significantly affects the conformations of the studied dehydropeptides. The tendency to adopt β-turn conformations is sign…
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…
Peptide p-nitrophenylanilides containing (E)-dehydrophenylalanine—synthesis, structural studies and evaluation of their activity towards cathepsin C
2006
Tetrapeptide p-nitroanilides containing (E)-dehydrophenylalanine were synthesized and evaluated as inhibitors and substrates of cathepsin C. Peptides containing a free, unblocked amino group appeared to be quite good substrates of the enzyme, whereas fully protected peptides acted as very weak inhibitors. Structural studies by means of NMR and CD, alongside with molecular modelling, have proved that these peptides are hydrolysed in one step by direct removal of p-nitroaniline from the tetrapeptide.
Effect of the ΔPhe residue configuration on a didehydropeptides conformation: A combined CD and NMR study.
2010
Conformations of two pairs of dehydropeptides with the opposite configuration of the ΔPhe residue, Boc-Gly-Δ(Z)Phe-Gly-Phe-OMe (Z-OMe), Boc-Gly-Δ(E)Phe-Gly-Phe-OMe (E-OMe), Boc-Gly-Δ(Z)Phe-Gly-Phe-p-NA (Z-p-NA), and Boc-Gly-Δ(E)Phe-Gly-Phe-p-NA (E-p-NA) were compared on the basis of CD and NMR studies in MeOH, trifluoroethanol (TFE), MeCN, chloroform, and dimethylsulfoxide (DMSO). The CD results were used as the additional input data for the NMR-based determination of the detailed solution conformations of the peptides. It was found that E-OMe is unordered and Z-OMe, Z-p-NA, and E-p-NA adopt the β-turn conformation. There are two overlapping β-turns in each of those peptides: type II and ty…
Synthesis of dehydrodipeptide esters and their evaluation as inhibitors of cathepsin C
2015
The procedures for the synthesis of esters of dehydropeptides containing C-terminal (Z)-dehydrophenylalanine and dehydroalanine have been elaborated. These esters appeared to be moderate or weak inhibitors of cathepsin C, with some of them exhibiting slow-binding behavior. As shown by molecular modeling, they are rather bound at the surface of the enzyme and are not submersed in its binding cavities. Electronic supplementary material The online version of this article (doi:10.1007/s00044-015-1366-0) contains supplementary material, which is available to authorized users.
Thymidylate synthases from Hymenolepis diminuta and regenerating rat liver: purification, properties, and inhibition by substrate and cofactor analog…
1995
Comparative studies of thymidylate synthases, isolated from the tapeworm, Hymenolepis diminuta, and regenerating liver of its host, rat, aimed at a possibility of specific inhibition of the helminthic enzyme, are presented. While similar in structure (dimers with monomer molecular masses of 33.7 kDa and 34.9 kDa, respectively) and parameters describing interactions with substrates and products, the tapeworm and rat enzymes differed in the dependences of reaction velocity on temperature (Arrhenius plots biphasic and linear, respectively). The tapeworm, compared with the host, enzyme was less sensitive to the competitive slow-binding inhibition by 5-fluoro-dUMP and its 2-thio congener, but eq…
Crystal structure ofN-(tert-butoxycarbonyl)glycyl-(Z)-β-bromodehydroalanine methyl ester [Boc–Gly–(β-Br)(Z)ΔAla–OMe]
2014
In a dehydroamino acid with a C=C bond between the α- and β-C atoms, the amino acid residues are linked trans to each other and there are no strong intramolecular hydrogen bonds. The torsion angles indicate a non-helical conformation of the molecule.
Conformation of tert-butoxycarbonylglycyl-dehydroalanyl-glycine methyl ester in the crystalline state and calculated in the gas phase.
2006
tert-Butoxycarbonylglycyl-dehydroalanyl-glycine methyl ester (systematic name: methyl {2-[(tert-butoxycarbonylamino)acetamido]prop-2-enamido}acetate) (Boc0-Gly1-ΔAla2-Gly3-OMe), C13H21N3O6, has been structurally characterized by single-crystal X-ray diffraction and by density functional theory (DFT) calculations at the B3LYP/6–311+G** level. The peptide chain in both the solid-state and calculated structures adopts neither β nor γ turns. All amino acid residues in the tripeptide sequence are linked trans to each other. The bond lengths and valence angles of the amino acid units in the crystal structure and gas phase are comparable. However, the conformation of the third glycyl residue (…
Synthesis of Hybrid Tripeptide Peptidomimetics Containing Dehydroamino Acid and Aminophosphonic Acid in the Chain and Evaluation of Their Activity to…
2021
Synthesis of a new group of hybrid phosphonodehydropeptides composed of glycyl-(Z)-dehydrophenylalanine and structurally variable aminophosphonates alongside with investigations of their activity towards cathepsin C are presented. Obtained results suggest that the introduction of (Z)- dehydrophenylalanine residue into the short phosphonopeptide chain does induce the ordered conformation. Investigated peptides appeared to act as weak or moderate inhibitors of cathepsin C.
Conformational studies of hexapeptides containing two dehydroamino acid residues in positions 3 and 5 in peptide chain
2008
Abstract Synthesis and structural studies of hexapeptides containing two dehydroamino acid residues in positions 3 and 5 in a peptide chain were performed. All the investigated peptides adopted bent conformations, stabilized by intramolecular hydrogen bonding, and could exist as two different conformers in solution. Only in the case of the peptide containing ΔAla residues, expected 3 10 -helical conformation was found.
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.
Conformational studies of hexapeptides containing two dehydroamino acid residues in positions 2 and 5 in peptide chain
2008
Conformational preferences of a group of hexapeptides containing two dehydroamino acid residues in Positions 2 and 5 in peptide chain were investigated by means of spectroscopic methods (NMR and CD) and theoretical calculations. In the case of dimethylsulfoxide (DMSO) solution, only peptide with free N-termini adopted rigid 310-helical conformation, for the rest of examined peptides extended and “zig-zag” conformers were predominant. CD measurements showed that only in chloroform solution the conformational freedom of investigated peptides was restricted. © 2008 Wiley Periodicals, Inc. Biopolymers 89: 691–699, 2008. This article was originally published online as an accepted preprint. The “…
Combined effect of the DeltaPhe or DeltaAla residue and the p-nitroanilide group on a didehydropeptides conformation.
2007
Two series of dehydropeptides of the general formulae Boc-Gly-X-Phe-p-NA, Boc-Gly-Gly-X-Phe-p-NA, Gly-X-Gly-Phe-p-NA·TFA, and Boc-Gly-X-Gly-Phe-p-NA, with X = ΔZPhe and ΔAla, were studied with NMR in DMSO and CDCl3-DMSO, and with CD in MeOH, MeCN, and TFE. The NMR spectra measured in DMSO suggest that peptides with the ΔPhe residue next to Phe are folded whereas peptides with Gly between ΔPhe and Phe are less ordered. NMR spectra of ΔAla-containing peptides indicate that these peptides are flexible and their conformational equilibria are populated by many different conformations. The CD spectra show that conformational properties of the peptides studied are distinctly influenced by a mutual…
CCDC 1814248: Experimental Crystal Structure Determination
2019
Related Article: Aneta Buczek, Dawid Siodłak, Maciej Bujak, Maciej Makowski, Teobald Kupka, Małgorzata A. Broda|2019|Struct.Chem.|30|1685|doi:10.1007/s11224-019-01387-w
CCDC 1529401: Experimental Crystal Structure Determination
2017
Related Article: Paweł Lenartowicz, Błażej Dziuk, Bartosz Zarychta, Maciej Makowski, Paweł Kafarski|2017|Phosphorus,Sulfur,Silicon,Relat.Elem.|192|706|doi:10.1080/10426507.2017.1308933
CCDC 1529397: Experimental Crystal Structure Determination
2017
Related Article: Paweł Lenartowicz, Błażej Dziuk, Bartosz Zarychta, Maciej Makowski, Paweł Kafarski|2017|Phosphorus,Sulfur,Silicon,Relat.Elem.|192|706|doi:10.1080/10426507.2017.1308933