Characterization of α-conotoxin interactions with the nicotinic acetylcholine receptor and monoclonal antibodies
| Autor: | D. James Ashcom, G. Bradley Stiles |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
animal structures
medicine.drug_class Molecular Sequence Data Mollusk Venoms Centrifugation Receptors Nicotinic Torpedo Monoclonal antibody Peptides Cyclic complex mixtures Biochemistry law.invention Lethal Dose 50 Mice law Conus medicine Animals Amino Acid Sequence Molecular Biology chemistry.chemical_classification biology Conus geographus Chemistry Antibodies Monoclonal Biological activity Cell Biology Fluoresceins biology.organism_classification Amino acid Solutions Dissociation constant Nicotinic acetylcholine receptor Spectrometry Fluorescence Chromatography Gel Binding Sites Antibody Conotoxins Research Article Protein Binding |
| Zdroj: | Biochemical Journal. 328:245-250 |
| ISSN: | 1470-8728 0264-6021 |
| DOI: | 10.1042/bj3280245 |
| Popis: | The venoms of predatory marine cone snails, Conus species, contain numerous peptides and proteins with remarkably diverse pharmacological properties. One group of peptides are the α-conotoxins, which consist of 13-19 amino acids constrained by two disulphide bonds. A biologically active fluorescein derivative of Conus geographus α-conotoxin GI (FGI) was used in novel solution-phase-binding assays with purified Torpedo californica nicotinic acetylcholine receptor (nAchR) and monoclonal antibodies developed against the toxin. The binding of FGI to nAchR or antibody had apparent dissociation constants of 10-100 nM. Structure-function studies with α-conotoxin GI analogues composed of a single disulphide loop revealed that different conformational restraints are necessary for effective toxin interactions with nAchR or antibodies. |
| Databáze: | OpenAIRE |
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