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Biomolecular Interaction Study of Cyclolinopeptide A with Human Serum Albumin
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 reactio...
| Autores principales: | , , , , |
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| Formato: | Texto |
| Lenguaje: | English |
| Publicado: |
Hindawi Publishing Corporation
2010
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| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3062964/ https://www.ncbi.nlm.nih.gov/pubmed/21436992 http://dx.doi.org/10.1155/2010/737289 |
| Sumario: | 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. |
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