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  • Polymer and Materials Science  (5)
  • solid-phase peptide-synthesis  (2)
  • 1995-1999  (7)
  • 1
    Electronic Resource
    Electronic Resource
    New synthetic tools for peptide-tetraphenylporphyrin derivatives (1998)
    Springer
    International journal of peptide research and therapeutics 5 (1998), S. 269-276 
    Details
    ISSN: 1573-3904
    Keywords: metalloenzymes ; peptide-porphyrins ; solid-phase peptide-synthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary New metal-tetraphenylporphyrins and Fmoc-lysine-metalloporphyrin derivatives have been used to prepare peptide-porphyrin and peptide-metalloporphyrin compounds via solid-phase peptide synthesis. A water-soluble peptide, covalently bound to a manganese(III)-porphyrin, has been used as a catalyst to promote the oxidation of ABTS by hydrogen peroxide ort-butylhydroperoxide.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02443544
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  • 2
    Electronic Resource
    Electronic Resource
    New Synthetic Tools for Peptide-Tetraphenylporphyrin Derivatives (1998)
    Springer
    International journal of peptide research and therapeutics 5 (1998), S. 269-276 
    Details
    ISSN: 1573-3904
    Keywords: metalloenzymes ; peptide-porphyrins ; solid-phase peptide-synthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract New metal-tetraphenylporphyrins and Fmoc-lysine-metalloporphyrin derivatives have been used to prepare peptide-porphyrin and peptide-metalloporphyrin compounds via solid-phase peptide synthesis. A water-soluble peptide, covalently bound to a manganese(III)-porphyrin, has been used as a catalyst to promote the oxidation of ABTS by hydrogen peroxide or t-butylhydroperoxide.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008869818565
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  • 3
    Electronic Resource
    Electronic Resource
    Discovering protein secondary structures: Classification and description of isolated α-turns (1996)
    New York : Wiley-Blackwell
    Biopolymers 38 (1996), S. 705-721 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Irregular protein secondary structures are believed to be important structural domains involved in molecular recognition processes between proteins, in interactions between peptide substrates and receptors, and in protein folding. In these respects tight turns are being studied in detail. They also represent template structures for the design of new molecules such as drugs, pesticides, or antigens. Isolated α-turns, not participating in α-helical structures, have received little attention due to the overwhelming presence of other types of tight turns in peptide and protein structures. The growing number of protein X-ray structures allowed us to undertake a systematic search into the Protein Data Bank of this uncharacterized protein secondary structure. A classification of isolated α-turns into different types, based on conformational similarity, is reported here. A preliminary analysis on the occurrence of some particular amino acids in certain positions of the turned structure is also presented. © 1996 John Wiley & Sons, Inc.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Solvent-mediated conformational transition in β-alanine containing cyclic peptides. VIIIprevious parts of this series are in Refs 1-7. (1996)
    New York : Wiley-Blackwell
    Biopolymers 38 (1996), S. 693-703 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: In the present paper we describe the solution nmr structural analysis and restrained molecular dynamic simulation of the cyclic pentapeptide cyclo-(Pro-Phe-Phe-β-Ala-β-Ala). The conformational analysis carried out in CD3CN and dimethylsulfoxide (DMSO) solutions by nmr spectroscopy was based on interproton distances derived from rotating frame nuclear Overhauser effect spectroscopy spectra and homonuclear coupling constants. A restrained molecular dynamic simulation in vacuo was also performed to build refined molecular models. The molecule is present in both solvent systems as two slowly interconverting conformers, characterized by a cis-trans isomerism around the β-Ala5-Pro1 peptide bond. In CD3CN solution, the conformer with a cis peptide bond is quite similar to that observed in the solid state, while the conformer containing all trans peptide bonds is characterized by an intramolecular hydrogen bond stabilizing a C10- and a C13-ring structure. In DMSO solution, the trans isomer is partly similar to that observed in CD3CN solution while the cis isomer is different from that observed in the solid state. The effect of the solvent in stabilizing different conformations was also investigated in DMSO-CD3CN solvent mixtures. © 1996 John Wiley & Sons, Inc.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Unusual conformational preferences of β-alanine containing cyclic peptides. VIIPrevious parts of this series are in Refs. 1-6. (1996)
    New York : Wiley-Blackwell
    Biopolymers 38 (1996), S. 683-691 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: In the present paper we describe the synthesis, purification, and single crystal x-ray analysis of the cyclic pentapeptide cyclo-(Pro-Phe-Phe-β-Ala-β-Ala). This compound crystallizes in the orthorhombic space group P212121 from methanol and adopts in the solid state an unusual conformation characterized by a cis β-Ala5-Pro1 peptide bond and by an intramolecular hydrogen bond stabilizing a C11- and a C12-ring structure. The C11, structure contains the Phe3 and the β-Ala4 at the corner position of the turn; it is the first observation of a type II β-turn enlargement due to the insertion of an extra methylene group of the β-alanine residue. The rest of the molecule participates in a newly characterized C12-ring structure, which incorporates a β-Ala residue at position i of the turn. © 1996 John Wiley & Sons, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360380602
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  • 6
    Electronic Resource
    Electronic Resource
    Bioactive peptides: Conformational studies of [TYR4] cyclolinopeptide A (1995)
    New York : Wiley-Blackwell
    Biopolymers 36 (1995), S. 453-460 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The solid state conformational analysis of [Tyr4] cyclolinopeptide A has been carried out by x-ray diffraction studies. The crystal structure of the monoclinic form, grown from a dioxane-water mixture [a = 9.849 (5) Å, b = 20.752 (4) Å, c = 16.728 (5) Å, β = 98.83 (3)°, space group P21, Z = 2], shows the presence of five intramolecular N-H- O=C hydrogen bonds, with formation of one C17 ring structure, one α-turn (C13), one inverse γ-turn (C7), and two β-turns (C10, one of type III and one of type 1). The Pro1-Pro2 peptide unit is cis (ω = 5°) all others are trans. The structure is almost superimposable with that of cyclolinopeptide A. The rms deviation for the atoms of the backbones is on the average 0.33 Å. © 1995 John Wiley & Sons, Inc.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360360408
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  • 7
    Electronic Resource
    Electronic Resource
    Solution conformational preferences of a peptidic analogue of a natural macrolide (1997)
    New York : Wiley-Blackwell
    Biopolymers 42 (1997), S. 349-361 
    Details
    ISSN: 0006-3525
    Keywords: cyclic peptides ; molecular dynamics ; nmr ; conformation ; FK506 ; FK506 binding proteins ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The conformational behavior in solution of a cyclic peptide with sequence cyclo-(Pro1-Pro2-Dab3 (cHexA)ψ[N7HCO]-Leu4ψ[NHCO]-Suc5-Gly6-) has been throughly investigated with the combined use of nmr and molecular dynamic techniques. The compound, which has been modeled to mimic the FK506 macrolide bound to the FK506 binding protein structure, can be considered as a peptidic analogue of the FK506 system.The synthesis was carried out on a phenylacetoamidomethyl resin using an appropriate protocol for the peptide chain elongation. The conformational properties of the cyclic hexapeptide were studied in DMSO and water. The nmr data in DMSO and restrained molecular dynamics simulations show the presence of two contiguous cis peptide bonds involving the -Gly-Pro-Pro- segment. This segment in water exhibits conformational heterogeneity presenting at least two distinct conformational families, characterized the first by cis-cis and the second by a trans-cis Gly-Pro-Pro configuration; the trans-cis isomer was fully characterized. © 1997 John Wiley & Sons, Inc. Biopoly 42: 349-361, 1997
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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