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  • 1
    Electronic Resource
    Electronic Resource
    Synthesis and Anaphylactogenicity of Monohaptenic Carbohydrate Conjugates (1983)
    New York, NY : Wiley-Blackwell
    Helvetica Chimica Acta 66 (1983), S. 1101-1109 
    Details
    ISSN: 0018-019X
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Peptidic model conjugates carrying a single 2-carboxy-4,6-dinitrophenyl haptenic group, and as carbohydrate moieties D-gluconoyl, β-D-mannopyranosyl, 2-deoxy-β-D-glucopyranos-2-yl, or lactobionoyl residues, including the pseudocarbohydrate residue 1,3,4,5-tetrahydroxycyclohexane-1-carbonyl, were synthesized. Conjugates carrying the lactobionoyl of the bis(2-deoxy-β-D-glucopyranos-2-yl) moiety were anaphylactogenic in the guinea pig, passively sensitized against 2-carboxy-4,6-dinitrophenyl antigen.
    Additional Material: 1 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/hlca.19830660413
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  • 2
    Electronic Resource
    Electronic Resource
    Preparation and Conformational Properties of Benzylpenicilloyl-oligo-L-lysine Conjugates (1982)
    New York, NY : Wiley-Blackwell
    Helvetica Chimica Acta 65 (1982), S. 1965-1971 
    Details
    ISSN: 0018-019X
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Selected oligo-L-lysine carriers and a poly-L-lysine were penicilloylated with benzylpenicillin. The resulting conjugates 2-6 were studied by IR. absorption in the solid state and circular dichroism measurements in solution. The IR. data demonstrate the lack of β-structure formation even in medium-sized peptides where such structures might be expected on the basis of previous studies on differently substituted oligo-L-lysines. Considerable proportions of right-handed α -helical conformation are exhibited by the icosa-L-lysine and poly-L-lysine conjugates 5 and 6 in water and 2,2,2-trifluoroethanol. Difficulties in obtaining fully penicilloylated conjugates are not related to the extent of α-helical conformation in aqueous solution.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/hlca.19820650703
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  • 3
    Electronic Resource
    Electronic Resource
    Monohaptenic Nα-Benzoyl-L-lysine Derivatives as Anaphylactogens: the Importance of the Unsubstituted Carboxyl Group (1984)
    New York, NY : Wiley-Blackwell
    Helvetica Chimica Acta 67 (1984), S. 1000-1002 
    Details
    ISSN: 0018-019X
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Nα-L-Iysine with a 2-carboxy-4, 6-dinitrophenyl (Dncp) haptenic group on the ε-amino function is a potent anaphylactogen in the guinea pig. We prepared Nε -Dncp- Nα-benzoly-L-Iysinamide and Nε-Dncp-Nα-benzoyl-L-lysyl-1-aminopropane where the carboxyl group of Iysine is blocked. Both compounds were non-elections of anaphylaxis.
    Additional Material: 1 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/hlca.19840670411
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  • 4
    Electronic Resource
    Electronic Resource
    (Cholestanyloxycarbonyl)benzyl esters as peptide substituents: Conformational properties of fully protected oligo-L-lysines with C-terminal (cholestanyloxycarbonyl)benzyl and benzyl ester moieties (1986)
    New York, NY : Wiley-Blackwell
    Helvetica Chimica Acta 69 (1986), S. 350-358 
    Details
    ISSN: 0018-019X
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: This study involves L-lysine oligo peptides, protected at the N-terminus by the Nps and at the ε-amino functions by Boc groups. Two series were prepared from dimer to octamer, one containing the p-[(cholestan-3β-yloxy)carbonyl]benzyl, the other one the benzyl ester group at the C-terminus. Conformational analyses were performed by IR absorption. The occurrence of the intermolecular β-structure in the solid state and in CH2Cl2 solution was demonstrated for the highest oligomers. The relative stabilities of the self-associated species were determined by adding a variety of polar solvents to the CH2Cl2 solutions. The cholestanyl-containing peptides have a lower propensity to self-aggregate than the benzyl-ester analogues. Self-aggregation and decreasing solubility run in parallel. It was also directly shown that soluble urea derivatives may disrupt intermolecular H-bonds in CH2Cl2, a point of practical interest, particularly in solid-phase peptide synthesis.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/hlca.19860690214
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  • 5
    Electronic Resource
    Electronic Resource
    Deblocking of o-Nitrophenylsulfenyl-Protected Peptides by Ammonium Thiocyanate and (2-Methyl-1-indolyl)acetic acid (1983)
    New York, NY : Wiley-Blackwell
    Helvetica Chimica Acta 66 (1983), S. 602-605 
    Details
    ISSN: 0018-019X
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The thiocyanate cleavage of the Na-o-nitrophenylsulfenyl group from peptides in solution or on a solid support proceeds effectively in the presence of (2-methyl-1-indolyl)acetic acid. This scavenger was prepared from 2-methylindole and sodium bromoacetate; it can readily be removed by extraction with base after the cleavage reaction, together with (2-methyl-3-(2-nitrophenylthio)-1-indolyl)acetic acid.
    Additional Material: 2 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/hlca.19830660219
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  • 6
    Electronic Resource
    Electronic Resource
    N-Acylureas in Peptide Synthesis: An X-Ray Diffraction and IR-Absorption Study (1990)
    New York, NY : Wiley-Blackwell
    Helvetica Chimica Acta 73 (1990), S. 626-634 
    Details
    ISSN: 0018-019X
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: An X-ray diffraction analysts of two N-acyl derivatives of symmetrical dialkylureas, N-[Nα-(benzyloxycarbonyl)-L-valyl] -N, N′-diisopropylurea (1) and N-{Nα(tert-butyloxy)carbonyl -L-valyl}-N-N′-dicyclohexylurea (2), and one N-acyl derivative of an unsymmetrical N-N′-dialkylurea, N-[Nα-(benzyloxycarbonyl)-L-valyl] -N′-(tert-butyl)-N-ethylurea (3), has been performed. It was established that it is the least hindered O-acylisourca N-atom that attacks intramolecularly the carbonyl group of the Nα-protected amino acid activated by the unsymmetrical carbodiimide to form the major rearrangement product. The occurrence and nature of intra- and intermolecularly H—bonded forms of the N-acylureas in the crystal state were also assessed. It was also shown that soluble N-acylureas may compete with intermolecular (peptide)N—H…O=C(peptide) H-bonds in CH2Cl2.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/hlca.19900730311
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  • 7
    Electronic Resource
    Electronic Resource
    Immunogenicity Studies with Haptenated Melittin Peptides: Implication for Membrane Involvement during the Recognition Step (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 2 (1996), S. 252-260 
    Details
    ISSN: 1075-2617
    Keywords: melittin immunogenicity ; antigen recognition ; membrane involvement ; haptenic position ; late IgG responses ; cellular dynamics ; Chemistry ; Biochemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Melittin peptides carrying 2,4-dinitro-6-carboxyphenyl (Dncp) haptenic groups regularly evoked anti-hapten IgG responses in mice or guinea pigs when the hapten was C-terminally attached. Single haptens on the N-terminal helix in several positions gave poor or no responses in the early stages but adequate titres after prolonged immunization. Peptides with Dncp at the C-terminus as an invariant feature and a second Dncp in various positions along the peptide chain did not fail to produce adequate responses. The hampering effect is not due to a defect at the T-cell level but involves the recognition step on the B-cell. It is implied that the haptenic interaction with the paratope of the recognizing immunoglob ulin on the B-cell involves the cell membrane in an important way. It is also suggested that late antibody responses should not be overlooked during the development of proteinaceous immunogens for vaccination.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/psc.74
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  • 8
    Electronic Resource
    Electronic Resource
    Molecular parameters in melittin immunogenicity (1997)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 3 (1997), S. 267-276 
    Details
    ISSN: 1075-2617
    Keywords: melittin immunogenicity ; T-cell epitopes ; human T-cell clone ; truncated melittin ; substituents on melittin ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Based on immunogenicity studies, two T-cell epitopes in melittin were found to be functional in guinea pigs, one being centrally located, the other one residing in the C-terminal chain. In Balb/c mice only the central epitope was found to be active. A human T-cell clone was found by T-cell proliferation studies to employ strictly the C-terminal chain. Truncation of melittin peptides at the N-terminus did not markedly affect the capacity of guinea pigs to develop anti-IgG responses towards peptidic epitopes and towards a C-terminally attached haptenic group. Attachment of various substituents inside and outside the T-cell epitopic areas had no marked effect on antibody responses. In contrast, the substituents positioned within a T-cell epitope abolished T-cell proliferation. This difference between whole animal data and cellular in vitro responses is presently not understood. © 1997 European Peptide Society and John Wiley & Sons, Ltd.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Aspects of Formation of the D-Penicillamine-Antigenic Determinant from Penicilloyl Compounds (1973)
    New York, NY : Wiley-Blackwell
    Helvetica Chimica Acta 56 (1973), S. 1235-1243 
    Details
    ISSN: 0018-019X
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The formation of D-penicillamine-L-cysteine mixed disulfide from benzylpenicilloic acid, benzylpenilloic acid and benzylpenicilloyl amide derivatives in L-cysteine suspensions at pH 7,6 and 37° was studied. The reaction is faster than direct penicilloylation of proteins known to be a route to penicilloyl antigenic determinants. The production of S-bound penicillamine on protein from penicilloyl compounds must therefore definitely be considered as a potential antigenforming step. The reaction may be partly if not fully blocked by acylation of the thiazolidine nitrogen of penicilloyl compounds. When formylation is applied a considerable reduction of the capacity of penicilloyl antigenic determinants to interact with anti-penicilloyl antibody is noted. A D-penicillamine-specific test antigen was prepared by binding D-penicillamine via thioether links to a partly succinylated poly-L-lysine. Clinical test reactions elicited with this conjugate and with penicilloic acid cannot be well correlated. Penicilloic acid probably detects reactions of undefined specificity in addition to D-penicillamine-specific ones.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/hlca.19730560408
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  • 10
    Electronic Resource
    Electronic Resource
    Immunogenicity of dinitrocarboxyphenylated melittin: The influence of C-terminal chain shortening, N-terminal substitution and prolin insertion at positions 5 and 10 (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 1 (1995), S. 140-148 
    Details
    ISSN: 1075-2617
    Keywords: Melittin immunogenicity ; T-cell epitopic secondary structure ; melittin toxicity ; substituent effects ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Peptides derived from the bee-venom melittin were fitted with the haptenic group dinitrocarboxyphenyl(Dncp) and tested in out-bred guinea pigs for immunogenicity by measuring the IgG anti-Dncp antibody response by ELISA. Dncp-conjugates comprising virtually the entire melittin proved to be strong immunogens producing antibody responses comparable to those of proteins. Weak responses were obtained with considerably shortened seqences. Conjugates with N-terminal Dncp gave markedly reduced antibody responses compared to peptides with C-terminal Dncp. An N-terminal biotinyl substituent abolished the immune response whereas N-terminal lauryl and caprylyl had little effect. Insertion of L-proline into a hexadecapeptide conjugate abolishing the possibility of helix formation gave an immunogen to which individual animals clearly responded on a low level. Oligomerisation, but not the cytolytic activity of melittin peptides, may contribute to the immunogenicities observed.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/psc.310010206
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