Abstract
The kinetics, energetics, and structure of Cyclolinopeptide A binding with Human Serum Albumin were investigated with surface plasmon resonance and circular dichroism. The complex is formed through slow recognition kinetics that is temperature sensitive in the range of 20°C-37°C. The overall reaction was observed to be endothermic (ΔH = 204 kJ mol(-1)) and entropy driven (ΔS = 746 J mol(-1)K(-1)) with overall small changes to the tertiary structure.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Circular Dichroism
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Dose-Response Relationship, Drug
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Flax / chemistry
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Humans
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Immobilized Proteins / chemistry
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Immobilized Proteins / metabolism
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Kinetics
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Peptides, Cyclic / chemistry
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Peptides, Cyclic / metabolism*
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Protein Binding
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Serum Albumin / chemistry
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Serum Albumin / metabolism*
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Surface Plasmon Resonance
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Thermodynamics
Substances
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Immobilized Proteins
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Peptides, Cyclic
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Serum Albumin
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cyclolinopeptide A