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  • 1
    ISSN: 1573-3904
    Keywords: Heterobifunctional resin ; Polystyrene-polyethylene glycol resin ; Immobilized peptides ; Confocal microscopy of peptide-resin beads ; Enzyme-linked immunosorbent assay
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary Fast and convenient binding assays using synthetic peptides are of utmost and increasing importance, especially in the search for lead structures or in the field of diagnostics. A polymeric support suitable for solid-phase peptide synthesis was functionalized with two different anchor groups. The interior part of the aminomethylated polystyrene-1%-divinylbenzene resin beads, comprising about 98% of the total loading capacity, was modified by the acid-labile ADPV anchor whereas the 2% outer surface of the polymer was covalently coated with a PEG 10 000 derivative which renders the resin surface hydrophilic and biocompatible. The novel resin was characterized by introducing marker amino acids and by infrared spectroscopy. Employing this bifunctionalized resin for peptide synthesis, free as well as polymer-bound peptides were obtained which were tested for recognition by antibody. The resin-bound peptides proved to be suitable for ELISA and fluorescence assays, as shown by confocal laser microscopic investigations. Peptides from the interior part were obtained in high yield and purity as analyzed by HPLC, electrospray mass spectrometry and Edman degradation.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    International journal of peptide research and therapeutics 6 (1999), S. 143-149 
    ISSN: 1573-3904
    Keywords: lactose permease ; neoglycopeptide ; 1-thio-β-d-galactoside ; transport inhibition
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary A new neoglycopeptide was synthesized and tested for its capability to bind to lactose permease ofEscherichia coli and to inhibit the transport of lactose. The free 5′-carboxypentyl-1-thio-β-d-galactopyranoside or the protected 2,3,4,6-tetra-O-acetyl-5′-carboxypentyl-1-thio-β-d-galactopyranoside was linked to the N-terminal α-amino group of the resin bound heptapeptide H-Phe-Phe-Gly-Gly-Gly-Gly-Ala-OH by different activation methods. Upon cleavage from the resin, deacetylation and purification, a neoglycopeptide which showed a significant inhibition of lactose permease was obtained.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    International journal of peptide research and therapeutics 6 (1999), S. 143-149 
    ISSN: 1573-3904
    Keywords: lactose permease ; neoglycopeptide ; 1-thio-β-D-galactoside ; transport inhibition
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract A new neoglycopeptide was synthesized and tested for its capability to bind to lactose permease of Escherichia coli and to inhibit the transport of lactose. The free 5′- carboxypentyl-1-thio-β-D-galactopyranoside or the protected 2,3,4,6-tetra-O-acetyl-5′-carboxypentyl-1-thio-β-D- galactopyranoside was linked to the N-terminal α-amino group of the resin bound heptapeptide H-Phe-Phe-Gly-Gly-Gly-Gly-Ala-OH by different activation methods. Upon cleavage from the resin, deacetylation and purification, a neoglycopeptide which showed a significant inhibition of lactose permease was obtained.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
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