Tobacco Mosaic Virus as a Carrier for Small Molecules. II. Cooperative affinity labeling of membrane vesicles with a TMV angiotensin conjugate. Preliminary communication

Kriwaczek, V. M.; Bonnafous, Jean‐Claude; Müller, Martin; Schwyzer, R.

doi:10.1002/hlca.19780610406

Cited by 15 publications

(1 citation statement)

References 8 publications

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“…The latter reaction allowed the separation of TMV-S-hormone/vesicle aggregates from unreacted virus particles and vesicles by density gradient centrifugation (Ref. 3). All of the observations suggested an especially strong, specific association between THy-S-hormone and receptors on the plasma membrane.…”

Section: Introductionmentioning

confidence: 95%

Hormone-receptor interactions: a study of the binding of hormone-substituted tobacco mosaic virus to membrane vesicles by dynamic light scattering and by transient electric bi-refringence

Schwyzer¹,

Kriwaczek²,

Baumann³

et al. 1979

Pure and Applied Chemistry

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-Tobacco mosaic virus has been covalently conjugated with 500 -600 molecules of different hormones. The particles react with antisera against the hormones and with hormone receptors in target organs, on target cells, and on membrane vesicles. The compounds were used for cooperative affinity labelling and for the isolation of receptor-bearing vesicles. The binding of a tobacco mosaic virus/angiotensin II conjugate to adrenal cortex membrane vesicles was studied by dynamic light scattering and transient electric birefringence. Despite the complexity of the polydisperse systems and the fact that the membrane vesicles exhibit a Kerr effect and depolarize the light, methods were developed that allowed the observation and theoretical treatment of the effects due to specific binding.

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Section: Introductionmentioning

confidence: 95%

Hormone-receptor interactions: a study of the binding of hormone-substituted tobacco mosaic virus to membrane vesicles by dynamic light scattering and by transient electric bi-refringence

Schwyzer¹,

Kriwaczek²,

Baumann³

et al. 1979

Pure and Applied Chemistry

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Tobacco mosaic virus as a carrier for small molecules: Artificial receptor antibodies and superhormones

Schwyzer

Kriwaczek

1981

Biopolymers

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SynopsisPeptide agonists covalently attached to tobacco mosaic virus exhibit such unusual properties as superpotency, superaffinity, enhanced resistance towards enzymic degradation, and prolonged action at the target cell. These properties can be exploited for the isolation by density-gradient centrifugation of membrane vesicles bearing specific receptors for the peptides and for radioactive and fluorescent labeling of cell-surface receptors. Our observations can be explained by cooperative-affinity phenomena caused by the deployment in space of the agonist molecules. DEPLOYMENT OF AGONIST MOLECULES AS A FACTOR IN BIOLOGICAL ACTIVITYSince early work on the conformation of cyclic peptides and on the organization of information in linear peptide agonists (for reviews, see Refs. 1-3), it has become increasingly clear that there exist causal relationships between the amino acid sequences of peptides, their conformational possibilities, their interactions with receptors, and their biological activity. In this review, we would like to point out the importance of another factor governing receptor interactions and biological activity, namely the deployment in space of groups of individual agonist molecules. Cooperative AffinityThe strong affinity of antibodies for membrane-bound antigens has been explained by the simultaneous binding of the two recognition sites on the antibody molecule to two antigen molecules connected through the membrane.4.5 Cooperative affinity effects of this type should prevail in any situation in which ligand and acceptor each possess more than one mutual recognition or binding site, provided that these sites are deployed in such a manner that simultaneous interaction is stereochemically feasible. A classical example of almost perfect complementarity is the DNA double helix, in which one single strand can be regarded as the ligand and the other as the acceptor molecule, both containing favorably deployed binding sites: the purine and pyrimidine bases.

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Immunoassays of peptide hormones and their chemical aspects

et al. 1983

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SynopsisThe N-terminal maleoyl-0-alanyl derivative of human gastrin-[2-17] has been synthesized as a model compound to investigate the usefulness of such peptide derivatives for their mild and selective conjugation, via reaction with thiol groups, to high-molecular-weight carrier molecules to produce antigens, as well as to radioiodinable or fluorogenic molecules to prepare tracers for immunoassays. In this context the examined enzyme substrate-gastrin conjugate was found to exhibit the full immunoreactivity of the parent peptide and to be well suited as tracer in a gastrin fluorescence-immunoassay.

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Tobacco Mosaic Virus as a Carrier for Small Molecules. II. Cooperative affinity labeling of membrane vesicles with a TMV angiotensin conjugate. Preliminary communication

Cited by 15 publications

References 8 publications

Hormone-receptor interactions: a study of the binding of hormone-substituted tobacco mosaic virus to membrane vesicles by dynamic light scattering and by transient electric bi-refringence

Hormone-receptor interactions: a study of the binding of hormone-substituted tobacco mosaic virus to membrane vesicles by dynamic light scattering and by transient electric bi-refringence

Tobacco mosaic virus as a carrier for small molecules: Artificial receptor antibodies and superhormones

Immunoassays of peptide hormones and their chemical aspects

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