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  • synthetic peptide  (4)
  • toxin-binding regions  (2)
  • 1
    Digitale Medien
    Digitale Medien
    Analysis of exposed regions on the main extracellular domain of mouse acetylcholine receptor α subunit in live muscle cells by binding profiles of antipeptide antibodies (1994)
    Springer
    The protein journal 13 (1994), S. 715-722 
    Details
    ISSN: 1573-4943
    Schlagwort(e): Antibody ; acetylcholine receptor ; synthetic peptide ; binding profile ; exposed regions
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Chemie und Pharmazie
    Notizen: Abstract To study the structural organization of the main extracellular domain of the nicotinic acetylcholine receptor (AChR)α subunit in live muscle cells, we examined the native membrane-bound receptors in cultured mouse skeletal muscle cells for their ability to bind a panel of antibodies against uniform-sized overlapping synthetic peptides which collectively represent this entire domain. The binding profile indicated that the regions α23–49,α78–126,α146–174, andα182–210 are accessible to binding with antibody. Residuesα23–49,α78–126, andα194–210 contain binding regions forα-neurotoxin and some myasthenia gravis autoantibodies. A comparison of this binding profile with the profile obtained for membrane-boundTorpedo californica AChR in isolated membrane fractions showed some similarities as well as significant differences between the subunit organization in the isolated membrane fraction and that in the membrane of live muscle cells. Regionsα89–104 andα158–174, which are exposed in the isolated membrane fraction, are also exposed in the live cell. On the other hand, regionsα23–49, andα182–210, which are exposed in the live cell, are not accessible in the isolated membrane and, furthermore, the regionα1–16, which has marginal accessibility in the cell, becomes highly accessible in the membrane isolates. The exposed regions defined by this study may be the primary targets for the initial autoimmune attack on the receptors in experimental autoimmune myasthenia gravis.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF01886954
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Amino acid substitutions outside a preselected antigenic region in hemoglobin affect the binding to monoclonal antibodies obtained by immunization with the synthetic region (1993)
    Springer
    The protein journal 12 (1993), S. 403-412 
    Details
    ISSN: 1573-4943
    Schlagwort(e): Monoclonal antibody ; synthetic peptide ; hemoglobin ; amino acid substitution ; antigenic site
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Chemie und Pharmazie
    Notizen: Abstract It is often assumed that amino acid substitutions outside a protein antigenic site have no effect on the reactivity of a protein variant with antibodies, especially monoclonal antibodies (mAbs). Substitutions that exert an effect on the reactivity of a protein variant with mAbs are frequently considered to be within the antigenic site of the mAb. To test this assumption, two mAbs [IgGl(k) and IgG2a (k)] were prepared by immunization with a synthetic peptide corresponding to region 63–78 of the α chain of human hemoglobin (Hb). The peptide was used as an immunogen in its free form (i.e., without conjugation to a carrier), so that the results will not be made ambiguous by peptide modification nor by an immune response to sites spanning peptide and protein carrier. In addition to their reaction with human Hb, the mAbs were also studied with four primate Hbs which had no substitutions within region α63–78 and only a limited number of substitutions which occurred outside of, and at considerable distances in three-dimensional (3D) structure from, this region. Inhibition studies revealed substantial differences in the binding affinities of some of the primate Hbs, relative to human Hb. Some of the substitutions caused major decreases in binding, although they were at considerable distances in the 3D structure from the indicated site residues. It is concluded that substitutions in a protein, even when distant from an antigenic site, can exert major influences on the protein's reactivity with anti-site mAbs.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF01025040
    Standort Signatur Erwartet Verfügbarkeit
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  • 3
    Digitale Medien
    Digitale Medien
    α-Neurotoxin binding to acetylcholine receptor: Localization of the full profile of the cobratoxin-binding regions on the α-chain ofTorpedo californica acetylcholine receptor by a comprehensive synthetic strategy (1987)
    Springer
    The protein journal 6 (1987), S. 365-373 
    Details
    ISSN: 1573-4943
    Schlagwort(e): acetylcholine receptor ; toxin-binding regions ; synthetic peptides ; cobratoxin
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Chemie und Pharmazie
    Notizen: Abstract Eighteen consecutive uniform overlapping synthetic peptides that spanned the entire extracellular part (residues 1–210) of the α-chain ofTorpedo californica acetylcholine receptor were screened for binding activity of125I-labeled cobratoxin. Five toxin-binding regions were localized within residues 1–10, 32–41, 100–115, 122–150, and 182–198. The five toxin-binding regions may be distinct sites or, alternatively, different faces in one or more sites.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF02343335
    Standort Signatur Erwartet Verfügbarkeit
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  • 4
    Digitale Medien
    Digitale Medien
    A novel peptide mimicking the interaction of α-neurotoxins with acetylcholine receptor (1987)
    Springer
    The protein journal 6 (1987), S. 455-461 
    Details
    ISSN: 1573-4943
    Schlagwort(e): α-bungarotoxin ; acetylcholine receptor ; synthetic peptide ; toxin-binding site
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Chemie und Pharmazie
    Notizen: Abstract A peptide corresponding to residues 26–41 of α-bungarotoxin, and closed by a disulfide bond between two cysteine residues at the amino and C terminal ends of the peptide, was synthesized and the monomeric form was purified. The peptide, which represents the exposed part of the long central loop of the toxin molecule, was examined for binding to acetylcholine receptor. The peptide was shown by radiometric titrations to bind radiolabeled receptor, and radiolabeled peptide was bound by receptor. The specificity of the binding was confirmed by inhibition with the parent toxin. A synthetic analog of the peptide in which Trp-28 was replaced by glycine had very little (10%) of the original activity. Succinylation of the amino groups of the peptide resulted in virtually complete (98%) loss of the binding activity. These results indicate that a shortened loop peptide corresponding to the region 26–41 of α-bungarotoxin exhibits binding activities mimicking those of the parent molecule. In this region, Trp-28, and one or both of Lys-26 and Lys-38, are essential contact residues in the binding to receptor.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF02343342
    Standort Signatur Erwartet Verfügbarkeit
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  • 5
    Digitale Medien
    Digitale Medien
    The regions of α-neurotoxin binding on the extracellular part of the α-subunit of human acetylcholine receptor (1988)
    Springer
    The protein journal 7 (1988), S. 173-177 
    Details
    ISSN: 1573-4943
    Schlagwort(e): acetylcholine receptor ; α-bungarotoxin ; cobratoxin ; α-neurotoxin ; synthetic peptides ; toxin-binding regions
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Chemie und Pharmazie
    Notizen: Abstract A set of 18 synthetic uniform overlapping peptides spanning the entire extracellular part (residues 1–210) of the α-subunit of human acetylcholine receptor were studied for their binding activity of125I-labeled α-bungarotoxin and cobratoxin. A major toxin-binding region was found to reside within peptide α122–138. In addition, low-binding activities were obtained with peptides α34–49 and α194–210. It is concluded that the region within residues α122–138 constitutes a universal major toxin-binding region for acetylcholine receptor of various species.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF01025247
    Standort Signatur Erwartet Verfügbarkeit
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  • 6
    Digitale Medien
    Digitale Medien
    Generation of species-specific antihemoglobin antibodies by immunization with synthetic peptides of human hemoglobin (1989)
    Springer
    The protein journal 8 (1989), S. 767-778 
    Details
    ISSN: 1573-4943
    Schlagwort(e): hemoglobin ; synthetic peptide ; fecal occult blood ; species identification ; antibodies
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Chemie und Pharmazie
    Notizen: Abstract Four peptides (7–16 residues) representing nonconserved regions of human hemoglobin (Hb) were selected for synthesis by comparison of the amino acid sequence of human Hb with those of the most common domesticated animals. Mouse antisera resulting from immunization with the synthetic peptides were investigated for binding to a panel of animal Hbs using solid-phase radioimmunoassay (RIA). One of the peptides elicited antibodies which bound specifically to human Hb, but not to any Hb of the nonprimate animals tested. The results show that the peptide immunogen chosen on the basis of dissimilarity between regions of different species is useful for the generation of species-specific antibodies. Such antibodies could serve as valuable tools for clinical screening of fecal occult blood trait and for forensic identification of bloodstains of human origin.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF01024901
    Standort Signatur Erwartet Verfügbarkeit
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