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  • 1
    Electronic Resource
    Electronic Resource
    Synthesis, characterization and biocompatibility of PEGA resins (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 1 (1995), S. 31-44 
    Details
    ISSN: 1075-2617
    Keywords: Synthesis resin ; beaded PEG polymer ; radical polymerization ; solid-phase peptide synthesis ; peptide library enzyme assay ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Three types of beaded polyethylene glycol polyacrylamide copolymers (PEGA) with a high content of polyethylene glycol (PEG) were synthesized by inverse suspension polymerization and characterized for peptide synthesis and with respect to their physical properties. Several peptides of high purity have been synthesized on the resin. The properties which were determined were loading of amino group, swelling, bead size distribution, porosity, flexibility and compatibility with active biomolecules. A loading of 0.35 mmol/g has been obtained and the swelling was excellent in solvents of various polarities ranging from water to dichloromethane. The 13C-NMR T1-relaxation times of a resin containing a peptide were determined in DMSO-d6 and the resin was found to exhibit a behaviour similar to the components in free solution.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/psc.310010106
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  • 2
    Electronic Resource
    Electronic Resource
    Preparation of fluorescence quenched libraries containing interchain disulphide bonds for studies of protein disulphide isomerases (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 4 (1998), S. 128-137 
    Details
    ISSN: 1075-2617
    Keywords: Disulphide bond formation ; fluorescence quenched library ; peptide library ; protein ; disulphide isomerase ; solid-phase assay ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Protein disulphide isomerase is an enzyme that catalyses disulphide redox reactions in proteins. In this paper, fluorogenic and interchain disulphide bond containing peptide libraries and suitable substrates, useful in the study of protein disulphide isomerase, are described. In order to establish the chemistry required for the generation of a split-synthesis library, two substrates containing an interchain disulphide bond, a fluoroescent probe and a quencher were synthesized. The library consists of a Cys residue flanked by randomized amino acid residues at both sides and the fluoroescent Abz group at the amino terminal. All the 20 natural amino acids except Cys were employed. The library was linked to PEGA-beads via methionine so that the peptides could be selectively removed from the resin by cleavage with CNBr. A disulphide bridge was formed between the bead-linked library and a peptide containing the quenching chromophore (Tyr(NO2)) and Cys(pNpys) activated for reaction with a second thiol. The formation and cleavage of the interchain disulphide bonds in the library were monitored under a fluoroescence microscope. Substrates to investigate the properties of protein disulphide isomerase in solution were also synthesized. © 1998 European Peptide Society and John Wiley & Sons, Ltd.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Inhibition of cruzipain visualized in a fluorescence quenched solid-phase inhibitor library assay. D-Amino Acid Inhibitors for cruzipain, cathepsin B and cathepsin L (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 4 (1998), S. 83-91 
    Details
    ISSN: 1075-2617
    Keywords: fluorescence quenched assay ; inhibitor library ; Trypanosoma cruzi ; cathepsin B and L inhibitors ; Parasitic protease inhibition ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A PEGA-resin was derivatized with a 3:1 mixture of hydroxymethyl benzoic acid and Fmoc-Lys(Boc)-OH and the fluorogenic substrate Ac-Y(NO2)KLRFSKQK(Abz)-PEGA was assembled on the lysine using the active ester approach. Following esterification of the hydroxymethyl benzoic acid with Fmoc-Val-OH a library XXX-k/r-XXXV containing approximately 200,000 beads was assembled by split synthesis. The resulting ‘one bead, two peptides’ library was subjected to extensive hydrolysis with cruzipain. One hundred darker beads were isolated and the 14 most persistently dark beads were collected and sequenced. The putative inhibitor peptides and several analogues were synthesized and found to be competitive μM to nM inhibitors of cruzipain in solution. The inhibitory activity was found to be unspecific to cruzipain when compared with cathepsins B and L and specific when compared with kallikrein. One of the inhibitors was docked into the active site of the cathepsin B and was found most probably to bind to the enzyme cavity in an unusual manner, owing to the inserted D-amino acid residue. © 1998 European Peptide Society and John Wiley & Sons, Ltd.
    Additional Material: 2 Ill.
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  • 4
    Electronic Resource
    Electronic Resource
    Multiple Column Synthesis of a Library of T-Cell Stimulating Tn-Antigenic Glycopeptide Analogues for the Molecular Characterization of T-Cell-Glycan Specificity (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 2 (1996), S. 212-222 
    Details
    ISSN: 1075-2617
    Keywords: mucin glycopeptides ; tumour associated antigen ; cancer ; MHC Class II binding ; glycopeptide synthesis ; Chemistry ; Biochemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A series of peptides and glycopeptides derived by amino acid and glycosyl amino acid scans through the self peptide from CBA/J mouse haemoglobin Hb (67-76), VITAFNEGLK, was synthesized by multiple column peptide synthesis (MCPS). Investigation of glycopeptide binding to the mouse major histocompatibility class II molecule Ek showed that glycans in position 72 did not interfere with the binding to Ek. Immunization experiments revealed that glycopeptides with the glycan in position 72 were immunogenic. Therefore a series of N-linked and O-linked glycopeptides with the glycan attached in the position 72 either to serine, threonine or asparagine was synthesized by MCPS. The glycan structure was furthermore varied with respect to monosacc haride component, size of oligosaccharide, anomer configuration and stereoche mistry of essential hydroxyl groups in order to investigate the specificity of the interaction with the T-cell receptor. Easy synthesis of ready to use Ser and Thr building blocks corresponding to mucin core 1, the Tn-antigen and its β-anomer were developed using trichloroacetimidates as glycosyl donors and reduction with in situ acetylation of the azide containing glycosylation products. Synthesis of an α-linked GlcNAc-Thr building block was achieved by glycosylation of Fmoc-Thr-OPfp with 2-azido-2-deoxy-3,4,6-tri-O-acetyl-D- glycopyranosyl trichloroacetimidate as a glycosyl donor. Other building blocks were obtained by previously described procedures.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/psc.64
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  • 5
    Electronic Resource
    Electronic Resource
    Synthetic hFSH peptide constructs in the evaluation of previous studies on the hFSH receptor interaction (1997)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 3 (1997), S. 397-414 
    Details
    ISSN: 1075-2617
    Keywords: computer modelling ; disulphide bond formation ; Fmoc solid-phase peptide synthesis ; hFSH ; hormone receptor interaction ; N-linked glycopeptide synthesis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The human follicle-stimulating hormone (hFSH) belongs to a family of glycoprotein hormones which contains two non-identical subunits. This paper describes the design and synthesis of a series of synthetic hFSH constructs as putative ligands for the receptor. The design of these constructs is based on the crystal structure of hCG and molecular modelling using the program package Insight II/Discover. The designed constructs contain peptides ranging from 7 to 48 amino acid residues, disulphide bridges and glycan residues. All the synthetic peptides were synthesized by the stepwise solid-phase method using Fmoc chemistry. Two of the synthetic peptides contain the glycosylated amino acid, Asn(GlcNAc-GlcNAc) and both were prepared using fully protected glycosylated building blocks in the solid-phase peptide synthesis. The disulphide bridges were formed from acetamidomethyl-protected glycopeptides and peptides by a direct deprotection/oxidation method using thallium(III) trifluoroacetate. Mass spectroscopy and amino acid analysis were used for characterization of the synthetic hFSH glycopeptides and peptides. The synthetic hFSH constructs were tested for binding activity on FSH receptor assays but none showed improved binding properties compared with the naturally occurring hormone. It was finally demonstrated that non-related peptides showed non-specific binding at the same level as reported for specific peptides. © 1997 European Peptide Society and John Wiley & Sons, Ltd.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    PEGA supports for combinatorial peptide synthesis and solid-phase enzymatic library assays (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 4 (1998), S. 195-210 
    Details
    ISSN: 1075-2617
    Keywords: PEGA ; solid-phase enzyme assay ; PEG ; MMP-9 ; fluorescence quenched peptides libraries ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Permeable resins cross-linked with long PEG chains were synthesized for use in solid-phase enzyme library assays. High molecular weight bis-amino-polyethylene glycol (PEG) 4000, 6000, 8000 were synthesized by a three-step reaction starting from PEG-bis-OH. Macromonomers were synthesized by partial or di-acryloylation of bis-amino-PEG derivatives. Bis/mono-acrylamido-PEG were copolymerized along with acrylamide by inverse suspension copolymerization to yield a less cross-linked resin (Type I, compounds 6-9). Furthermore, acryloyl-sarcosin ethyl ester was co-polymerized along with bis-acrylamido PEG to obtain more crosslinked capacity resin (Type II, compounds 13-19). N,N-Dimethylacrylamide was used as a co-monomer in some cases. The polymer was usually obtained in a well-defined beaded form and was easy to handle under both wet and dry conditions. The supports showed good mechanical properties and were characterized by studying the swelling properties, size distribution of beads, and by estimating the amino group capacity. Depending on the PEG chain length, the monomer composition and the degree of cross-linking the PEGA supports showed a high degree of swelling in a broad range of solvents, including water, dichloromethane, DMF, acetonitril, THF and toluene; no swelling was observed in diethyl ether. The PEGA resins (Type I) with an amino acid group capacity between 0.07 and 1.0 mmol/g could be obtained by variation of the monomer composition in the polymerization mixture. Fluorescent quenched peptide libraries were synthesized on the new polymer using a multiple column library synthesizer and incubated with the matrix metalloproteinase MMP-9 after it had been activated by 4-aminophenyl mercuric acetate resulting in 67/83 kDa active enzyme. The bright beads were separated manually under a fluorescence microscope and sequenced to obtain peptide substrates for MMP-9. After treatment with ethylene diamine, high-loaded resins (Type II) have been employed in continuous flow peptide synthesis to yield peptides in excellent yield and purity. © 1998 European Peptide Society and John Wiley & Sons, Ltd.
    Additional Material: 7 Ill.
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  • 7
    Electronic Resource
    Electronic Resource
    Fluorescent properties of amino acids labeled with ortho-aminobenzoic acid (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 4 (1998), S. 395-402 
    Details
    ISSN: 1075-4261
    Keywords: ortho-aminobenzoylamino acids ; fluorescence ; protease ; peptide ; peptide synthesis ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: ortho-Aminobenzoic acid (Abz) has been used as a convenient fluorescent donor group in internally quenched fluorescent peptides, which are employed as substrates for several proteolytic enzymes. As Abz is usually bound to the N-amino terminal of these peptides, it is of interest to investigate the Abz group fluorescent properties bound to different amino acids. We report in this article the optical absorption and fluorescent properties, in aqueous media, of Abz bound to the α-amino group of Ala, Gly, Leu, Ile, Val, Pro, Phe, Arg, Glu, Met, Asn, Tyr, and Trp, with monomethyl-amidated α-carboxyl group. In order to explore the origin of the drastic reduction of Abz attached to Nα amino group of prolyl-peptides, we also examined the fluorescence properties of Abz-NHCH3, Abz-N(CH3)2, and Abz-pyrrolidine. Molecular dynamics simulation and NMR data indicated a lack of periplanarity of the Abz-dimethylamide, which could be the origin of low fluorescence quantum yield of Abz-prolyl-peptides. © 1998 John Wiley & Sons, Inc. Biospectroscopy 4: 395-402, 1998
    Additional Material: 2 Ill.
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  • 8
    Electronic Resource
    Electronic Resource
    Direkte Festphasen-Glycosylierung von Peptiden an einem neuartigen Polyethylenglycol-HarzDiese Arbeit wurde von der Europäischen Union gefördert (Grant SCI*-CT920765). (1997)
    Weinheim : Wiley-Blackwell
    Zeitschrift für die chemische Industrie 109 (1997), S. 2064-2067 
    Details
    ISSN: 0044-8249
    Keywords: Festphasensynthesen ; Glycopeptide ; Glycosylierungen ; Verbindungsbibliotheken ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ange.19971091814
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  • 9
    Electronic Resource
    Electronic Resource
    Eine neue Strategie zur Festphasensynthese von O-GlycopeptidenDiese Arbeit wurde von der Studienstiftung des Deutschen Volkes und der Stiftung Stipendien-Fonds des Verbandes der Chemischen Industrie gefördert. (1992)
    Weinheim : Wiley-Blackwell
    Zeitschrift für die chemische Industrie 104 (1992), S. 881-883 
    Details
    ISSN: 0044-8249
    Keywords: Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ange.19921040719
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  • 10
    Electronic Resource
    Electronic Resource
    Eine neue Strategie zur Festphasensynthese von O-Glycopeptiden über 2-Azidoglycopeptide (1994)
    Weinheim : Wiley-Blackwell
    Liebigs Annalen 1994 (1994), S. 369-379 
    Details
    ISSN: 0170-2041
    Keywords: O-Glycopeptides ; Solid-phase synthesis ; Galactose, 2-azido-2-deoxy-D- ; Peptides ; Carbohydrates ; Azido sugars ; Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A New Strategy for the Solid-Phase Synthesis of O-Glycopeptides via 2-Azido-glycopeptidesThe building blocks Fmoc-Thr(α-D-GalN3Ac3)-OPfp (8) and Fmoc-Ser(α-D-GalN3Ac3)-OPfp (9) were synthesized. Both building blocks are active esters which can directly be used for the solid-phase synthesis of O-glycopeptides. The obtained glycopeptides carry an 2-azido-2-deoxy-D-galactosyl residue α-linked to Thr or Ser. The conversion of the 2-azido into the 2-acetamido groups was achieved with thioacetic acid on solid support, and subsequently the sugar residues of the polymer bound glycopeptides were deacetylated with hydrazine hydrate in methanol. The subsequent cleavage from the resin with TFA/water gave after RP-HPLC purification directly the desired deprotected O-glycopeptides.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jlac.199419940410
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