Studies of the influence of different cross-linking reagents on the immune response against a B-epitope

Delmas, A.F.; Brack, A.; Trudelle, Y.

doi:10.1021/bc00013a013

Cited by 4 publications

(2 citation statements)

References 17 publications

(14 reference statements)

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“…The haptenation of protein for the purpose of raising antibodies to small molecules such as drugs or toxins influences the immune response at the T-cell level (1). The production of antibody is sterically influenced by the site of attachment between drug and carrier molecule.…”

Section: Introductionmentioning

confidence: 99%

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Optimization and Immunological Characterization of a Photochemically Coupled Lysergic Acid Diethylamide (LSD) Immunogen

Kerrigan

Brooks

1998

Bioconjugate Chem.

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A photoreactive heterobifunctional linker was used to prepare an immunogen in which lysergic acid diethylamide was indirectly coupled to keyhole limpet hemocyanin at multiple sites on the drug. It was possible to attach approximately 35 drug molecules to each protein using approximately equal amounts of both species during the reaction. The presence of buffer components or water severely compromised reaction efficiency, as estimated from the molar substitution ratio. Factors such as excess linker, pH, irradiation of dry matrix in the absence of buffer, and the drug/protein ratio used during photolysis were shown to have pronounced effects on reaction efficiency. Structural insights regarding immunogen coupling were obtained by determining the specificities of antibodies which were raised against the immunogen. Cross-reactivity data indicated that haptenation of protein likely occurred at positions N1 and N6 of lysergic acid diethylamide, which is plausible given the electrophilicity of the photogenerated aryl nitrene.

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Section: Introductionmentioning

confidence: 99%

“…Lysergic acid diethylamide (LSD) 1 is a controlled drug which is abused for its potent psychoactive properties. A typical dose is only between 50 and 100 µg as a result of its unusually high potency, relative to other common hallucinogens such as psilocybin or mescaline.…”

Section: Introductionmentioning

confidence: 99%

Optimization and Immunological Characterization of a Photochemically Coupled Lysergic Acid Diethylamide (LSD) Immunogen

Kerrigan

Brooks

1998

Bioconjugate Chem.

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Synthesis, conformation, and immunoreactivity of new carrier molecules based on repeated tuftsin‐like sequence

et al. 2004

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Sequential oligopeptides based on a pentapeptide (TKPKG) derived from tuftsin with different lengths were synthesized by stepwise solid phase methodology. These highly soluble oligomers were nontoxic on mouse spleen cells, and other biological data suggested that tuftsin-like properties were also presented. The (TKPKG)n (n=2,4,6,8) oligopeptides were not immunogenic; however, they increased sheep red blood cells (SRBC) antigen specific antibody response in mice, demonstrating their immunostimulatory effect. Chemotactic activity was also found on J774 monocyte cells, while MRC5 fibroblasts were chemotactically nonresponders to the tested forms of tuftsin. These oligomers showed unordered and flexible structure by CD measurements, confirmed by computer modeling studies indicating also a fairly good accessibility of the epsilon-amino group of each lysine residue. Data suggest that these new oligotuftsin derivatives can be considered as promising carriers for synthetic vaccine.

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Tuftsin: On the 30-year anniversary of Victor Najjar’s discovery

Siemion

Kluczyk

1999

Peptides

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Studies of the influence of different cross-linking reagents on the immune response against a B-epitope

Cited by 4 publications

References 17 publications

Optimization and Immunological Characterization of a Photochemically Coupled Lysergic Acid Diethylamide (LSD) Immunogen

Optimization and Immunological Characterization of a Photochemically Coupled Lysergic Acid Diethylamide (LSD) Immunogen

Synthesis, conformation, and immunoreactivity of new carrier molecules based on repeated tuftsin‐like sequence

Tuftsin: On the 30-year anniversary of Victor Najjar’s discovery

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