Abstract
This study utilized the E. coli expression system to investigate the role of amino acid residues in toxin from the Chinese scorpion--Buthus martensii Karsch (BmKAS). To evaluate the extent to which residues of the toxin core contribute to its analgesic activity, ten mutants of BmKAS were obtained by PCR. Using site-directed mutagenesis, all of these residues were substituted with different amino acids. This study represents a thorough mapping and elucidation of the epitopes that form the molecular basis of the toxin's analgesic activity. Our results showed large mutant-dependent differences that emphasize the important roles of the studied residues.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
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Validation Study
MeSH terms
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Analgesics, Non-Narcotic / chemistry*
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Analgesics, Non-Narcotic / pharmacology*
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Animals
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Insect Proteins / chemistry*
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Insect Proteins / genetics
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Insect Proteins / pharmacology*
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Mice
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Models, Molecular
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Mutagenesis, Site-Directed
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Mutant Proteins / chemistry
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Mutant Proteins / isolation & purification
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Mutant Proteins / pharmacology
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Neurotoxins / chemistry
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Neurotoxins / genetics
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Neurotoxins / pharmacology
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Pain Measurement
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Peptides / chemistry*
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Peptides / genetics
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Peptides / pharmacology*
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Protein Conformation
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Protein Interaction Mapping
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Protein Structure, Tertiary
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Recombinant Proteins / chemistry
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / pharmacology
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Scorpion Venoms / chemistry*
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Scorpion Venoms / genetics
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Scorpion Venoms / pharmacology*
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Scorpions / metabolism*
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Sequence Alignment
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Sequence Homology, Amino Acid
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Structure-Activity Relationship
Substances
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Analgesics, Non-Narcotic
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Insect Proteins
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KAS toxin, Buthus martensi Karsch
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LqhIT2 insect toxin
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Mutant Proteins
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Neurotoxins
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Peptides
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Recombinant Proteins
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Scorpion Venoms