Chemical Synthesis and Structure-Function Studies of Margatoxin, a Potent Inhibitor of Voltage-Dependent Potassium Channel in Human T Lymphocytes
| Autor: | Randal M. Bugianesi, Maria A. Bednarek, Reid J. Leonard, John P. Felix |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Charybdotoxin
Stereochemistry T-Lymphocytes Xenopus Potassium Molecular Sequence Data Neurotoxins Biophysics Scorpion Venoms chemistry.chemical_element Peptide medicine.disease_cause Biochemistry Chemical synthesis Protein Structure Secondary Membrane Potentials chemistry.chemical_compound Potassium Channel Blockers medicine Animals Humans Amino Acid Sequence Disulfides Molecular Biology Cells Cultured chemistry.chemical_classification Sequence Homology Amino Acid Toxin Margatoxin Metalloendopeptidases Cell Biology T lymphocyte Potassium channel chemistry Oocytes |
| Zdroj: | Biochemical and Biophysical Research Communications. 198:619-625 |
| ISSN: | 0006-291X |
| Popis: | The 39 amino acid peptide, margatoxin (MgTX), a potent inhibitor of the voltage-activated potassium channel (Kv1.3) in human T lymphocytes, was synthesized by a solid phase technique. Formation of the disulfide bridges was rapid at pH 8.2. The final product was purified to homogeneity and was physically and biologically indistinguishable from the toxin prepared biosynthetically. The disulfide bridge pairing was similar to that found previously for the related toxin - charybdotoxin (3): from Cys7 to Cys29, from Cys13 to Cys34 and from Cys17 to Cys36. Eight analogs of MgTX were synthesized and tested for inhibition of 125I margatoxin binding to voltage-activated potassium channels. The results indicate that the three C-terminal residues of MgTX are important for the efficient toxin binding to Kv1.3. |
| Databáze: | OpenAIRE |
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