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  • 11
    Digitale Medien
    Digitale Medien
    T CELL RECOGNITION OF LYSOZYME IV. LOCALIZATION AND GENETIC CONTROL OF THE CONTINUOUS T CELL RECOGNITION SITES BY SYNTHETIC OVERLAPPING PEPTIDES REPRESENTING THE ENTIRE PROTEIN CHAIN (1984)
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 11 (1984), S. 0 
    Details
    ISSN: 1744-313X
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie , Medizin
    Notizen: Recently, this laboratory has developed a comprehensive strategy for the systematic localization of all the ‘continous’ antigenic (as well as other binding) sites of complex multivalent protein antigens involved in B and T cell recognition. The strategy depends on the syntheis of consecutive overlapping peptides that together account for the entire protein chain. This strategy was applied here for the localization of the ‘continuous’ T cell recognition sites of hen egg lysozyme. Eight overlapping peptides encompassing the entire protein chain of lysozyme were synthesized and examined for their ability to stimulate in vitro proliferation of T cells from several mouse strains (A/J, H-2a; BALB/c and DBA/2, H-2d; B10.BR, H-2k; DBA/1, H-2a; SJL, H-2s) that had been primed with native lysozyme. This approach enabled the identification of a full profile of in vitro active lysozyme peptides and the localization of four major T cell recognition sites, three of which were subject to individual control.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1744-313X.1984.tb00819.x
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  • 12
    Digitale Medien
    Digitale Medien
    III. RECOGNITION OF THE ‘SURFACE-SIMULATION’ SYNTHETIC ANTIGENIC STIES (1984)
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 11 (1984), S. 0 
    Details
    ISSN: 1744-313X
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie , Medizin
    Notizen: In previous studies from this laboratory the antigenic sites of lysozyme were found to be composed of spatially adjacent surface residues that are mostly distant in sequence (i.e. discontinuous sites). For synthetic mimicking of the sites, we introduced the concept of ‘surface-simulation’ synthesis by which the binding site residues are linked directly via peptide bonds with appropriate spacing and directionality into a single peptide which does not exist in the protein but mimics a surface region of it. In the present report T cell recognition of the surface-simulation synthetic antigenic sites has been explored in a mouse strain, B10.BR, that is a high responder to lysozyme. The discontinuous antigenic sites of lysozyme also had the capacity to stimulate proliferation of T cells driven by native lysozyme in long-term cultures. Thus, in addition to the four continuous T sites that we have recently reported, T cell recognition of lysozyme also involves discontinuous sites. This is the first clear demonstration that, contrary to a long-held impression, T cell recognition is not restricted only to sequence features, but can also be directed to protein discontinuous surface areas of high conformational dependency.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1744-313X.1984.tb01060.x
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  • 13
    Digitale Medien
    Digitale Medien
    Effects of amino acid substitutions outside an antigenic site on protein binding to monoclonal antibodies of predetermined specificity obtained by peptide immunization: Demonstration with region 94–100 (antigenic site 3) of myoglobin (1992)
    Springer
    The protein journal 11 (1992), S. 433-444 
    Details
    ISSN: 1573-4943
    Schlagwort(e): Amino acid substitutions ; monoclonal antibodies ; myoglobin ; predetermined specificity ; synthetic antigenic site
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Chemie und Pharmazie
    Notizen: Abstract Amino acid substitutions outside protein antigenic sites are very frequently assumed to exert no effect on binding to antiprotein antibodies, especially if these are monoclonal antibodies (mAbs). In fact, a very popular method for localization of residues in protein antigenic sites is based on the interpretation that whenever a replacement causes a change in binding to antibody, then that residue will be located in the antigenic site. To test this assumption, mAbs of predetermined specificity were prepared by immunization with a free (i.e., without coupling to any carrier) synthetic peptide representing region 94–100 of sperm whale myoglobin (Mb). The cross-reactivities and relative affinities of three mAbs with eight Mb variants were studied. Five Mb variants which had no substitutions within the boundaries of the designed antigenic site exhibited remarkable, and in two cases almost complete, loss in cross-reactivity relative to the reference antigen, sperm whale Mb. Two myoglobins, each of which had one substitution within region 94–100, showed little or no reactivity with the three mAbs. It is concluded that substitutions outside an antigenic site can exert drastic effects on the reactivity of a protein with mAbs against the site and that caution should be exercised in interpreting cross-reactivity data of proteins to implicate residues directly in an antigenic site.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF01025020
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  • 14
    Digitale Medien
    Digitale Medien
    Mapping the extracellular topography of the α-chain in free and in membrane-bound acetylcholine receptor by antibodies against overlapping peptides spanning the entire extracellular parts of the chain (1994)
    Springer
    The protein journal 13 (1994), S. 37-47 
    Details
    ISSN: 1573-4943
    Schlagwort(e): Antipeptide antibodies ; acetylcholine receptor ; polypeptide chain organization ; subunit topography ; synthetic peptides
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Chemie und Pharmazie
    Notizen: Abstract The extracellular surface of theα-chain ofTorpedo california acetylcholine receptor (AChR) was mapped for regions that are accessible to binding with antibodies against a panel of synthetic overlapping peptides which encompassed the entire extracellular parts of the chain. The binding of the antipeptide antibodies to membrane-bound AChR (mbAChR) and to isolated, soluble AChR. was determined. The specificity of each antiserum was narrowed down by determining the extent of its cross-reaction with the two adjacent peptides that overlap the immunizing peptide. With mbAChR, high antibody reactivity was obtained with antisera against peptidesα1–16,α89–104,α158–174,α262–276, andα388–408. Lower, but significant, levels of reactivity were obtained with antibodies against peptidesα67–82,α78–93,α100–115, andα111–126. On the other hand, free AChR bound high levels of antibodies against peptidesα34–49,α78–93,α134–150,α170–186, andα194–210. It also bound moderate levels of antibodies against peptidesα262–276 andα388–408. Low, yet significant, levels of binding were exhibited by antibodies against peptidesα45–60,α111–126, andα122–138. These binding studies, which enabled a comparison of the accessible regions in mbAChR and free AChR, revealed that the receptor undergoes considerable changes in conformation upon removal from the cell membrane. The exposed regions found here are discussed in relation to the functional sites of AChR (i.e., the acetylcholine binding site, the regions that are recognized by anti-AChR antibodies, T-cells and autoimmune responses and the regions that bind short and long neurotoxins).
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF01891991
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  • 15
    Digitale Medien
    Digitale Medien
    Antigenic structure of human hemoglobin: Delineation of the antigenic site (site 2) within region 41–65 of the alpha chain by immunochemistry of synthetic peptides (1985)
    Springer
    The protein journal 4 (1985), S. 171-184 
    Details
    ISSN: 1573-4943
    Schlagwort(e): hemoglobin ; α chain ; antigenic structure ; antigenic site ; synthetic peptides
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Chemie und Pharmazie
    Notizen: Abstract A comprehensive synthetic approach consisting of a series of consecutive, uniform overlapping peptides encompassing the entire protein chain was recently used to determine the full antigenic profile of the α-chain of human hemoglobin (Hb). The peptides synthesized enabled the localization of five major “continuous” antigenic regions within the α chain. The present findings describe the delineation of an antigenic site (site 2) residing within the region 41–65. Ten peptides representing the α-chain regions 41–55, 51–65, 45–54, 45–56, 45–58, 45–60, 48–56, 49–56, 50–56, and 51–56 were synthesized and purified. Quantitative radioimmunoadsorbent titrations were used to determine binding to peptide adsorbents of radioiodinated anti-Hb antibodies that were raised in rabbit, goat, and outbred mouse. In one set of peptides, the N-terminal was fixed while the C-terminal end was increased by increments of two residues from Gln-54 to Lys-60 (i.e., peptides 45–54, 45–45, 45–58, and 45–60). Binding studies revealed that maximum antibody activity resided in peptide 45–45, indicating that Lys-56 marks the C-terminal boundary of the site. In the second set of peptides, the C-terminal was fixed at Lys-56 while the peptides were elongated at their N-terminal by one-residue increments from Gly-51 to Leu-48. Antibody-binding studies with these peptides indicated that Ser-49 defines the N-terminal boundary of the site. Therefore, the antigenic site within region 41–65 of the α chain comprises residues 49–56. The relevance of these findings to the immune recognition of Hb and other proteins is discussed.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF01025263
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  • 16
    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
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  • 17
    Digitale Medien
    Digitale Medien
    Synthesis of tolerogenic monomethoxypolyethylene glycol and polyvinyl alcohol conjugates of peptides (1991)
    Springer
    The protein journal 10 (1991), S. 623-627 
    Details
    ISSN: 1573-4943
    Schlagwort(e): Antibody response ; epitope-specific suppression ; monomethoxypolyethylene glycol ; polyvinyl alcohol ; tolerogenic peptide conjugate
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Chemie und Pharmazie
    Notizen: Abstract Recent studies from this laboratory showed that tolerogenic peptide conjugates are very effective reagents for obtaining epitope-specific immunosuppression of antibody responses to immunopathogenic sites on multideterminant complex protein antigens. This paper describes the procedure for synthesis of well-defined conjugates of peptides to monomethoxypoly-ethylene glycol (mPEG) or to polyvinyl alcohol (PVA). The first step involves succinylation of the hydroxyl groups on the polymers by reaction with succinic anhydride. The polymer is then coupled via the carboxyl of the succinyl group to the α-NH2 of the completed peptide on the synthetic resin, while maintaining intact all the side-chain protecting groups on the peptide. The mPEG or PVA-peptide conjugates are cleaved from the resin and purified by standard procedures. This method results in the preparation of conjugates in which one molecule of tolerogenic polymer is coupled to the N-terminal of an otherwise unaltered peptide molecule.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF01025714
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  • 18
    Digitale Medien
    Digitale Medien
    Mapping by synthetic peptides of the binding sites for acetylcholine receptor on α-bungarotoxin (1988)
    Springer
    The protein journal 7 (1988), S. 655-666 
    Details
    ISSN: 1573-4943
    Schlagwort(e): α-bungarotoxin ; acetylcholine receptor ; synthetic peptides ; toxin-binding sites
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Chemie und Pharmazie
    Notizen: Abstract A set of seven peptides constituting the various loops and most of the surface areas of α-bungarotoxin (BgTX) was synthesized. In appropriate peptides, the cyclical (by a disulfide bond) monomers were prepared. In all cases, the peptides were purified and characterized. The ability of these peptides to bindTorpedo californica acetylcholine receptor (AChR) was studied by radiometric adsorbent titrations. Three regions, represented by peptides 1–16, 26–41, and 45–59, were able to bind125I-labeled AChR and, conversely,125I-labeled peptides were bound by AChR. In these regions, residues Ile-1, Val-2, Trp-28 and/or Lys-38, and one or all of the three residues Ala-45, Ala-46, and Thr-47, are essential contact residues in the binding of BgTX to receptor. Other synthetic regions of BgTX showed little or no AChR-binding activity. The specificity of AChR binding to peptides 1–16, 26–41, and 45–59 was confirmed by inhibition with unlabeled BgTX. It is concluded that BgTX has three main AChR-binding regions (loop I with N-terminal extension and loops II and III extended toward the N-terminal by residues 45–47).
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF01024881
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  • 19
    Digitale Medien
    Digitale Medien
    Subunit Interacting Surfaces of Human Hemoglobin in Solution: Localization of the α–β Subunit Interacting Surfaces on the α-Chain by a Comprehensive Synthetic Strategy (1999)
    Springer
    The protein journal 18 (1999), S. 179-185 
    Details
    ISSN: 1573-4943
    Schlagwort(e): Hemoglobin ; α–β chain association ; oligomeric proteins ; synthetic peptides ; subunit interacting surfaces
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Chemie und Pharmazie
    Notizen: Abstract By using synthetic overlapping peptides encompassing the entire α-chain of adult human hemoglobin (HbA), we have mapped on the α-chain the regions responsible for its binding to the β-chain in solution. These binding surfaces were, in general, in good agreement with those expected from the crystal structure (peptides α81–95, α101–115, α111–125, and α131–141). However, we observed some significant differences in the levels of binding found here in solution and those expected from the crystal structure. Peptide α31–45, which in the crystal had the highest number of contact residues of all the α-chain peptides, did not bind the β-chain in solution. Similarly, peptide α91–105, with seven contact residues in the crystal, showed low binding with the β-chain in solution. On the other hand, peptides α41–55 and α121–135 possessed much higher binding activity in solution than would be expected from their contribution to subunit association in the crystal. In fact, peptide α121–135 had the highest binding activity of the α-chain peptides. These studies and our previous findings, which localized on the β-chain the regions that bind to the α-chain in solution, have shown that the regions of subunit association in solution are close to, but not identical with, those in the crystal. The approach should be quite useful for mapping subunit association in oligomeric proteins and could even be applied to proteins that are isolated only in traces or whose three-dimensional structure is not yet known.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1023/A:1020623905544
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  • 20
    Digitale Medien
    Digitale Medien
    Localization and synthesis of an insulin-binding region on human insulin receptor (1990)
    Springer
    The protein journal 9 (1990), S. 229-233 
    Details
    ISSN: 1573-4943
    Schlagwort(e): Insulin ; insulin receptor ; binding site ; synthetic peptides
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Chemie und Pharmazie
    Notizen: Abstract Seven regions of the α subunit of human insulin receptor (HIR) were synthesized and examined for their ability to bind radioiodinated insulin. A peptide representing one of these regions (namely, residues α655–670) exhibited a specific binding activity for insulin. In quantitative radiometric titrations, the binding curves of125I-labeled insulin to adsorbents of peptide α655–670 and of purified placental membrane were similar or superimposable. The binding of radioiodinated insulin to peptide or to membrane adsorbents was completely inhibited by unlabeled insulin, and the inhibition curves indicated that the peptide and the membrane on the adsorbents had similar affinities. Synthetic peptides that were shorter (peptide α661–670) or longer (peptide α651–670) than the region α655–670 exhibited lower insulin-binding activity. It was concluded that an insulin-binding region in the HIR α subunit resides within residues α655–670. The results do not rule out the possibility that other regions of the α subunit may also participate in binding of HIR to insulin, with the region described here forming a “face” within a larger binding site.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF01025313
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